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Curriculum of M.Sc. Biochemistry From Academic Year 2017-2018 Onwards Department of Biochemistry Bharathidasan University- Trichy

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Page 1: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

Curriculum of M.Sc. Biochemistry

From Academic Year 2017-2018 Onwards

Department of Biochemistry

Bharathidasan University- Trichy

Page 2: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

Programme Outcomes

• PG Granduands are Professionally Competent with characteristic Knowledge-bank, Skill-

set, Mind-set and Pragmatic Wisdom in their chosen fields.

• PG Granduands demonstrate the desired sense of being Seasoned and exhibit unequivocal

Spiritedness with excellent qualities of productive contribution to society and nation in the

arena Science and Technology.

• PG Graduands are mentored such that they exert Leadership Latitude in their chosen fields

with commitment to novelty and distinction.

• PG Graduants are directed in understanding of ethical principles and responsibilities, moral

and social values in day-to-day life thereby attaining Cultural and Civilized personality.

• PG Graduants of are able to Collate information from different kinds of sources and gain a

coherent understanding of the subject.

Page 3: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

PROGRAM SPECIFIC OUTCOME

1. The course aims in gaining an understanding of the processes of metabolic

transformation at the molecular level and how these processes are studied.

2. It is important to study enzymes, the rate limiting molecule of all the chemical

reactions and understanding enzymes could pave research ideas.

3. Students can make the Knowledge of the relationship between structure and function

at organ and/or organism level, of important cell biological communication

principles and processes, and how they are regulated.

4. Students can able to Characterize certain functionalities of biomolecules by using

spectroscopic technique

5. Students will gain conceptual understanding of subject matter, scientific reasoning

skills, laboratory manipulative skills.

6. The course aims to give participants a basic knowledge of mechanisms of signal

transduction and the significance of signal transduction in physiology and

pathophysiology.

7. Students can understand the capacity to evaluate and synthesise information from a

wide range of sources in order to communicate ideas, concepts and construct

arguments in both non-scientific and scientific language.

8. Students will learn at the end of the course to conserve the nature and will be able to

develop new strategies to preserve the sources of life.

Page 4: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

DEPARTMENT OF BIOCHEMISTRY

DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES

BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI 620 024

M.Sc. DEGREE PROGRAMME IN BIOCHEMISTRY (SEMESTER PATTERN-AUTONOMOUS)

CHOICE BASED CREDIT SYSTEM – (CBCS) (For the candidates admitted from the academic year 2017-18 onwards)

REGULATIONS

1. Name of the Programme

Bharathidasan University is offering a two-year M.Sc. Degree Programme in

Biochemistry to be conducted in the Department of Biochemistry, School of Life

Sciences, Bharathidasan University.

2. Eligibility for admission to the Programme

A candidate who has passed B.Sc. Degree Examination of Bharathidasan

University with Biochemistry/ Chemistry / Zoology /Botany / Nutrition &

Dietetics / Food Science/ Microbiology / Biotechnology as the Major subject or

an examination of any other University accepted by the Syndicate of

Bharathidasan University as equivalent to the B.Sc. degree examination of

Bharathidasan University may be permitted to qualify for the M.Sc. Degree in

Biochemistry by undergoing courses and appear for the examinations of this

Department. A candidate for admission to the programme shall not be more

than 25 years of age as on 1st July of the year of admission.

3. Duration of the Programme

The Programme is for a period of two years. Each year shall consist of two

semesters namely Odd and Even semesters. Odd semesters shall commence

from July and even semesters from December. There shall not be less than 90

working days which shall comprise 450 teaching hours for each semester

(exclusive of the days for the conduct of University end-semester examinations).

4. Scheme of the Examination

I. There shall be examinations at the end of each semester, for odd semesters in the month of October / November; for even semesters in April / May.

II. A candidate who does not pass the examination in any course(s) may be permitted to appear in such failed course (s) in the subsequent examinations to be held in October / November or April / May. However candidates who have arrears in Practicals shall be permitted to take their arrear Practical examination only along with Regular Practical examination in the respective semester.

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III. A candidate should get registered for the first semester examination. If registration is not possible owing to shortage of attendance beyond condonation limit / regulation prescribed OR belated joining OR on medical grounds, the candidates are permitted to move to the next semester. Such candidates shall re-do the missed semester after completion of the course.

IV. Viva-Voce: Each candidate shall be required to appear for Viva-Voce Examination (in defence of the Project only).

V. For the Project Report, the maximum marks will be 75 per cent and for the Viva-Voce it is 25 per cent.

VI. A candidate who could not earn credits in certain course(s) of the first,

second and third semesters will be permitted to appear in such course(s)

along with the courses in any subsequent semester examination.

Semester Courses

I

4 Core Courses

1 Laboratory Course

II

2 Core Courses

1 Elective Course

1 ED Course

1 Laboratory Course

III

2 Core Courses

1 Elective Course

1 ED Course

1 Laboratory Course

IV

1 Project

* ED : Extra Disciplinary

➢ The Core Courses (CC), Laboratory courses (LC) and Elective Courses

(EC) will be offered by the Department of Biochemistry and ED course

(EDC) shall be offered by the various Departments of the University

➢ The failed candidates in one EC / EDC are permitted to opt for another EC /

EDC Or they are permitted to continue with the same EC / EDC.

Page 6: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

➢ The maximum marks for the examination conducted for each course

is 100, out of which 75 is for University Examination (UE) and 25 is

for Continuous Internal Assessment (CIA).

➢ Grade “AAA” means absent for the UE for the course.

➢ The number of contact hours per week for any course shall range

from three to six hours.

➢ The examinations will be conducted by the Department.

➢ Duration for UE for theory shall be three hours and for practical three

to six hours.

➢ To qualify for the degree, the candidate has to earn at least 72 credits

by way of earning at least 44 credits in Core courses, at least 6 credits

in the Elective courses, 4 credits in ED courses and 18 credits in the

Project Work mentioned above.

➢ The content of the syllabus for each course is divided into six units

and the sixth unit is been excluded for examination. However, the

topic will be discussed on the regular class hours.

➢ In the case of courses with practical component, 75 is for University

Practical Examination (UE) and 25 is for Continuous Internal

Assessment (CIA).

➢ The syllabi will be framed by the Board of Studies consisting of all the

members of the faculty in the Department and experts from outside

the department (approved by the University) with Head of the

Department as the Chairperson.

➢ There is no provision for improvement of marks in UE and CIA in any

course.

➢ In the statement of marks, both the mark obtained by the candidate

and the grade awarded to him/her will be mentioned.

➢ The whole programme must be completed within 4(four) years from

the date of joining; otherwise the registration for the programme will

be cancelled.

5. Project

Each candidate shall be required to take up a Project Work; submit Project

Report at the end of the second year. The Head of the Department shall assign

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the Guide who in turn will suggest the Project Work to the student in the

beginning of fourth semester. Two typed copies of the Project Report shall be

submitted to the Department on or before the date fixed by the Department

Head.

The Dissertation will be evaluated by Examiners, nominated by the Department.

The candidate concerned will have to defend his project in a Viva-Voce

examination

6. Credits

The term “Credit‟ refers to the weightage given to a course, usually in relation to

the instructional hours assigned to it. For instance, a six hour course is assigned

four credits, four/ five hour course is assigned three credits and two hour

course is given two credits. However, in no instance the credits of a course can

be greater than the hours allotted to it.

The total minimum credits, required for completing a PG programme is 72. The

details of credits for individual components and individual courses are given in

Table.

7. Attendance

➢ Every student should put in at least 75% attendance in each course.

➢ In each semester every candidate must compulsorily register for the

examination in all the courses attended in that semester.

➢ No candidate who has put in attendance for less than 75% of the

working days in a semester will be permitted to take the UE pertaining

to that semester unless he/she gets condonation certificate.

➢ On the day, on which a course is concluded, the Course Teacher of the

course shall intimate the Head of the Department the particulars of all

students who have shortage of attendance in the course offered by

him/her.

➢ A candidate who has put in less than 65% attendance in a course,

he/she has to either repeat the course or take an equivalent course.

➢ Condonation of shortage of attendance shall be given as per the

provisions given below:

Page 8: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

o Students must have 75% of attendance in each course for appearing

the examination. Students who have 74% to 70% of attendance shall

apply for condonation in the prescribed form with the prescribed fee

of Rs.500/- (Rupees Five hundred only). Students who have 69% to

65% of attendance shall apply for condonation in prescribed form

with the prescribed fee of Rs.500/- (Rupees Five hundred only) along

with the Medical Certificate.

o Students who have below 65% of attendance are not eligible to

appear for the examination. They shall re-do the semester(s) after

completion of the programme.

o The Head of the Department shall announce the names of all students

who will not be eligible to take the end-semester examination in the

various courses due to shortage of attendance.

8. Question Paper Pattern Part A

Ten Questions ( No choice) 10 x 2 = 20 marks Two Questions from each Unit

Part B Five Questions (either or type) 5 x 5 = 25 marks

One Question from each Unit Part C

Three Questions out of five 3 x 10 = 30 marks One Question from each unit

9. Evaluation

The performance of a student in each course is evaluated in terms of

percentage of marks with a provision for conversion to grade points.

Evaluation for each course shall be done by a continuous internal

assessment by the concerned Course Teacher as well as by an end

semester examination and will be consolidated at the end of the course.

The components for continuous internal assessment are :

Two tests - 15 Marks (Third / repeat tests for genuine absentees)

Seminar - 5 Marks

Assignments - 5 Marks

--------------

Total: 25 Marks

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--------------

Attendance need not be taken as a component for continuous

assessment, although the students should put in a minimum of 75%

attendance in each course. In addition to continuous evaluation

component, the end semester examination, which will be a written-

examination of at least 3 hours duration, would also form an integral

component of the evaluation. The ratio of marks to be allotted to

continuous internal assessment and to end semester examination is 25 :

75. The evaluation of laboratory component, wherever applicable, will

also be based on continuous internal assessment and on an end-semester

practical examination.

10. Passing Minimum

➢ A candidate shall be declared to have passed in each course if he/she

secures not less than 40% marks in the University Examinations and

40% marks in the Internal Assessment and not less than 50% in the

aggregate, taking Continuous assessment and University Examinations

marks together.

➢ Failed candidates in the Internal Assessment are permitted to improve

their Internal Assessment marks in the subsequent semesters (2

chances will be given) by writing the CIA tests and by submitting

assignments.

➢ Candidates, who have secured the pass marks in the end-semester

Examination (U.E.) and in the C.I.A. but failed to secure the aggregate

minimum pass mark (E.S.E. + I.A.) are permitted to improve their

Internal Assessment mark in the following semester and / or in

University Examinations.

➢ A candidate shall be declared to have passed in the Project work if

he/she gets not less than 40% in each of the Project Report and

Viva/Voce but not less than 50% in the aggregate of both the marks for

Project Report and Viva-Voce.

➢ A candidate who gets less than 40% in the Project Report must

resubmit the Project report.

Page 10: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

➢ Such candidates need to take the Viva-Voce on the resubmitted Project.

11. Letter Grade and Grade Points of the Courses and Final Result

Once the marks of the CIA and end-semester examinations for each of the

course are available, they will be added. The marks, thus obtained will

then be graded as per the scheme provided in the following Table.

Grade Point Letter Grade

96 and above 10 S+

91-95 9.5 S

86-90 9.0 D++

81-85 8.5 D+

76-80 8.0 D

71-75 7.5 A++

66-70 7.0 A+

61-65 6.5 A

56-60 6.0 B

50-55 5.5 C

Below 50 0 F

From the second semester onwards the total performance within a

semester and continuous performance starting from the first semester are

indicated respectively by Grade Point Average (GPA) and Cumulative

Grade Point Average (CGPA). These two are calculated by the following

formulae:

n

∑CiGi

i = 1

GPA = ------------------------

n

∑Ci

i = 1

Page 11: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

Where ‘Ci’ is the Credit earned for the Course i in any semester; ‘Gi’ is the

Grade Point obtained by the student for the Course i and ‘n’ is the number

of Courses passed in that semester. CGPA = Average Grade Points of all the

Courses passed starting from the first semester to the current semester.

Page 12: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

Final Result

* Absence from an examination shall not be taken as an attempt.

12. Instant Examination

The department will conduct instant examination to a candidate in May/June if

only one course remains to be cleared by him/her to qualify for the degree.

13. Revision of Regulations and Curriculum

The Department from time to time revise, amend and change the regulations

and the curriculum, if found necessary.

CGPA Letter Grade Classification of Final Result

9.51 and

above

S+

First Class - Exemplary

9.01-9.50 S

8.51-9.00 D++

First Class – Distinction 8.01-8.50 D+

7.51-7.50 D

6.51-7.00 A++

First Class 6.01-6.50 A+

5.51-6.00 A

5.00-5.50 B Second Class

5.00-5.50 C

Below 5.00 F Fail

Page 13: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

DEPARTMENT OF BIOCHEMISTRY

SCHOOL OF LIFE SCIENCES

BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI 620 024

M.Sc. DEGREE PROGRAMME IN BIOCHEMISTRY (CBCS)

(For the candidates to be admitted from the year 2017-18 onwards)

Semester Courses

I

4 Core Courses

1 Laboratory Course

II

2 Core Courses

1 Elective Course

1 ED Course

1 Laboratory Course

III

2 Core Courses

1 Elective Course

1 ED Course

1 Laboratory Course

IV

1 Project

Page 14: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

DEPARTMENT OF BIOCHEMISTRY, BHARATHIDASAN UNIVERSITY,

TIRUCHIRAPPALLI-24

M.Sc. Biochemistry Course Structure (2017 – 2018 onwards)

SEM Category Code Courses Hrs Crs

I

Core 1 BC101 Biomolecules 6 6

Core 2 BC102 Enzymes 6 6

Core 3 BC103 Cell and Molecular Biology 6 6

Core 4 BC104 Biochemical Techniques 6 6

Core 5 BC105 Laboratory Courses-I 6 4

Total for Semester-I 30 28

II

Core 6 BC 201 Biochemistry of Signal Transduction & Regulation 6 6

Core 7 BC 202 Intermediary Metabolism 6 6

Elective BC 203 Elective- I 5 3

Core 8 BC 204 Laboratory Courses –II 6 4

Non major

Elective

BC2ED ED-I 3 2

Total for Semester II 26 21

III

Core 9 BC 301 Immunology 6 6

Core 10 BC 302 Genetic Engineering and Molecular Techniques 6 6

Elective BC 303 Elective - II 5 3

Core 11 BC 304 Laboratory Courses -III 6 4

Non major

Elective

BC3ED ED-II 3 2

Total for Semester III 26 21

IV

BC 401 Project & Viva Voice 30 20

Total for Semester IV 30 20

Total hours & credits 112 90

Page 15: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

Elective

BC203 Ecology and Environmental Biology

BC205 Bioinformatics

BC206 Biostatistics

BC207 Chromatin and Epigenetics

BC303 Clinical Biochemistry

BC305 Membrane Biochemistry

BC306 Concept in Neurochemistry

Non Major Elective

BC3ED Developmental Biology

BC2ED Genetics

BC3ED-I Computational Biology

Page 16: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

BC101 - BIOMOLECULES

(Core 1)

SEM: I Lecture/Week: 6

BC101 Credits: 6

Objectives

i. To list out the structure and functions of biological macromolecules.

ii. To learn the metabolism and integration of biomolecules that takes place in human

system.

iii. Integrate the various aspects of metabolism and their regulatory pathways

iv. Students can understand the fundamental energetics of biochemical processes

v. To elaborate the relation between biochemical defects and metabolic disorders.

vi. To enumerate the organization of signalling pathways.

UNIT- I

HOMO AND HETEROGLYCANS: Polysaccharides - occurrence, structure, properties

and functions of homoglycans - starch, glycogen, cellulose, dextrin, inulin, chitin, xylans

and galactans. Occurrence, structure, properties and functions of heteroglycans - hyaluronic

acid, keratan sulphate and chondroitin sulphate. Bacterial cell wall polysaccharides, Blood

group substances, Sialic acid. Glycoproteins and their biological functions. Lectins structure

and functions. ( https://biologydictionary.net/polysaccharide)

Unit - II

PROTEINS: Classification, structure and properties of amino acids, Essential and non-

essential amino acids. Non protein amino acids. Proteins - Classification based on solubility,

shape, composition and function. Properties of proteins. Denaturation and renaturatton of

proteins. Structure of peptide bonds. Chemical synthesis of polypeptides. Protein structure -

Primary, secondary, tertiary and quaternary structures of protein. Forces stabilizing the

secondary, tertiary and quaternary structures of proteins. Structure and biological functions

of fibrous proteins (keratins, collagen and elastin), globular proteins (hemoglobin,

myoglobin), lipoproteins, metalloproteins, glycoprotein and nucleoproteins.(chalk and talk)

Unit - III

LIPIDS: Definition and classification of lipids. Fatty acids - classification, nomenclature,

structure and properties. Triacylglycerols. Classification, structure and function of

prostaglandins, thromboxanes and leukotrienes. Chemical properties and functions of

phospholipids and their structures - lecithins, cephalins, phosphatidyl serine, phosphatidyl

inositol, plasmalogens. Glycolipids (cerebrosides and gangliosides), Isoprenoids and sterols

(cholesterol and zymosterol), steroids (steroid hormones), bile acids and bile salts. Types

and functions of plasma lipoproteins. (https://www2.chemistry.msu.edu/faculty/reusch/virttxtjml/lipids.htm)

Unit - IV

NUCLEIC ACIDS: Structure of purines and pyrimidines. Components of nucleic acids -

nucleosides, nucleotides, and poly nucleotides. Occurrence and isolation of nucleic acids.

Page 17: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

Properties of DNA: buoyant density,viscosity, hypochromicity, denaturation and

renaturation– the cot curve. Chemical synthesis of oligonucliotides. DNA: structure of

different types (A, B and Z DNA), biological role, polymorphism. Structure and role of

different types of RNA. (Problem based learning*)

UNIT-V

VITAMINS AND PORPHYRINS: Structure and biochemical properties of water soluble

and fat soluble vitamins and their coenzyme activity. Macro minerals (Ca, P, Mg, Na, K, Cl)

and micro minerals/trace elements (Co, I, Fe, Mn, Zn, and F) - their sources, daily

requirements, functions and deficiency diseases symptoms. Porphyrins the porphyrin ring

system, chlorophyll, hemoglobin, myoglobin and cytochrome.

Unit VI:

Advanced studies in various metabolic pathways and significance of macromolecules,

Enzymatic control of metabolic pathways, Metabolic profiles of key tissues, Hormonal

control of pathways.

Recommended Books:

1) L. Stryer. 2002. Biochemistry, 5th edition. W.H.Freeman & Company, New York

2) Horton, R., Moranm, LA., Scrimgeour, G, MarcPerry and David Rawn. 2006.

Principles of Biochemistry, 4th edition.

3) A. L. Lehninger, Nelson & Cox. 2007. Principles of Biochemistry, 5th edition, CBS,

India.

4) Murray R. K. et al. Harpers Illustrated Biochemistry, 2009, 28th edition. Lange

Medical Books/McGraw-Hill.

5) Zubay, 2005. Principles of Biochemistry, 4th edition. Prentice hall.

6) Richard Harvey, Denise Ferrier. 2005. Lippincott. Outlines of Biochemistry, 5th

edition.

COURSE OUTCOME:

i) To understand the structure and functions of biological macromolecules.

ii) To learn the metabolism and integration of biomolecules that takes place in human

system

iii) Integrate the various aspects of metabolism and their regulatory pathways

iv) Students can understand the fundamental energetics of biochemical processes

v) "To understand the relation between biochemical defects and metabolic

disorders."

vi) To understand the organization of signalling pathways.

vii) To understand the role of membrane processes in metabolism

viii) "Overall, gaining an understanding of the processes of metabolic

transformation at the molecular level and how these processes are studied. "

Page 18: Curriculum of M.Sc. Biochemistry From Academic Year 2017 ... · DEPARTMENT OF BIOCHEMISTRY DST-FIST SPONSORED DEPARTMENT SCHOOL OF LIFE SCIENCES BHARATHIDASAN UNIVERSITY, TIRUCHIRAPPALLI

BC 102 – ENZYMES

(Core 2)

SEM: I Lecture/Week: 6

BC102 Credits: 6

Objectives:

i. Students will obtain basic knowledge about the relationship between properties and

structure of the enzymes, their mechanism of action and kinetics of enzymatic

reactions.

ii. The student could able to analyse the structure/function relationships in biocatalysed

reactions

iii. The student would able to describe the priciples and methods of metabolic

engineering of (micro) organisms to produce industrial chemicals.

iv. Students able to research a contemporary application of enzyme technology or

metabolic engineering and present the results in a well-structured oral

presentation.

v. Students can understand to compare and contrast the historical uses of enzyme

technology with current applications in a diverse range of industries.

Unit - I

Introduction of enzymes: definitions (catalytic power, specificity, reactivity, regulation,

transformation of different forms of energy, Holoenzyme, Apoenzyme, coenzymes and

cofactors). Enzyme Nomenclature and IUB system of enzyme classification. Active site-

Fisher and Koshland models. Formation of enzyme substrate complex evidences. Basic

concepts of bioenergetics: The collision theory, activation energy and transition state theory.

Measurement and expression of enzyme activity – enzyme assays, Investigation of sub-

cellular compartmentation of enzymes and marker enzymes. Enzyme units.

(https://www.medicalnewstoday.com/articles/319704.php)

Unit- II

Enzyme kinetics: Pre-Steady state and Steady state kinetics, Rapid reaction kinetics

(Continuous flow and stopped flow techniques). Kinetics of single substrate enzyme

catalyzed reaction - Michaelis-Menten (Briggs- Haldane) equation, Double-Reciprocal Plot,

Lineweaver Burk plot, Eadie-Hofstee and Hanes-Wolf plots. Determination of Vmax, Km,

Kcat, Specificity constant (Kcat/Km) and their significance. Factors influencing enzymatic

activity, Arrhenius plot. Kinetics of enzyme reactions having two or more substrates. Single

displacement and double displacement reactions.(chalk and talk)

Unit - III

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Enzyme inhibition: Reversible and Irreversible inhibition - Competitive, Non-competitive

and mixed inhibition. Substrate inhibition and Feedback inhibition.Determination of

inhibitor constant.Therapeutic, diagnostic and industrial applications of enzyme

inhibitors.Mechanism of enzyme action: Factors contributing to the catalytic efficiency -

proximity and orientation, covalent catalysis, acid-base catalysis, metal ion catalysis, strain

and distortion theory. Mechanism of action of Lysozyme, Carboxy peptidase, Chymotrypsin

and Ribonuclease.( elte.prompt.hu/sites/default/files/tananyagok/.../ch09s04.htm)

Unit IV:

Introduction of co-enzymes: Structure and functions – Pyridine and flavin nucleotides,

coenzyme A, Pyridoxal phosphate and thiamine pyrophosphate, tetrahydrofolate and B12

coenzymes. Allosteric Interactions: Enzyme regulation, allosteric enzymes. Allosteric

kinetics (MWC and KNF models), symmetry and sequential models. Hill’s equation and

Hill’s co-efficient. Enzyme repression and covalent modification of enzymes. Zymogen

activation. Isozymes.

Unit V:

Multienzyme system: Multifunctional enzymes. Multi-enzyme complexes (Pyruvate

dehydrogenase complex, fatty acid synthase and Na - K ATPase), Oligomeric enzymes and

Metalloenzymes. Modern concepts of evolution of catalysts: Catalytic RNA (Ribozymes),

abzymes. Immobilized enzymes and their industrial applications. Chemical modification and

site-directed mutagenesis of enzymes. Industrial applications of enzymes - food and

pharmaceutical enzymes. Biosensors. (blended mode of teaching *)

Unit VI:

Enzyme Structure Activity Relationship (SAR) and Drug Discovery- Properties of

Enzymes: Lead Compound, Structure based drug design, combinatorial chemistry, High-

throughput screening, Case study of DHFR.

Recommended Books:

1. Principles of Biochemistry, 1993. A.L. Lehninger, Nelson & Cox (CBS, India) and

new edition.

2. Biochemistry, 2004, Donald Voet and Judith Voet, John Wiley and sons. ISBN -

047119350

3. Biochemistry, 5th edition, by Lubert Stryer, New York: W H Freeman; 2002, ISBN-

10: 0-7167-3051-0.

4. Text Book of Biochemistry with clinical correlations, 4th edition – Thomas M.

Devlin.

5. Text of Biochemistry, 1908 – West & Todd, MacMillian Publications

6. Principles of Biochemistry, by G. L. Zubay, 1995, Wm. C. Brown

7. Biochemistry 2nd edition Christopher K.Mathews and K.E.VanHoldge (1995)

(Benjamin and cumming).

8. Enzymes. Dixon and Webb 3rd ed. Longmans, 1979.

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9. Enzymes in Food Technology. CRC Press, 2001. Whitehurst RJ.

10. Industrial Enzymes and their applications. Uhlig H. John Wiley, 1998.

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COURSE OUTCOME:

i) Students will obtain basic knowledge about the relationship between properties and

structure of the enzymes, their mechanism of action and kinetics of enzymatic

reactions.

ii) The student could able to analyse the structure/function relationships in biocatalysed

reactions

iii) The student would able to describe the priciples and methods of metabolic engineering

of (micro)organisms to produce industrial chemicals.

iv) Students able to research a contemporary application of enzyme technology or

metabolic engineering and present the results in a well-structured oral presentation.

v) Students can understand to compare and contrast the historical uses of enzyme

technology with current applications in a diverse range of industries.

vi) At the end of the course students will be explored to understand the use of enzymes in

medicine, food, organic synthesis, genetics and other areas sectors that favor a wide

reach for them.

vii) To integrate the practical aspects of enzymology with the kinetic theories to provide a

mechanistic overview of enzyme activity and regulation in cells

viii) It is important to study ezymes,the rate limiting molecule of all the chemical reactions

and understanding enzymes could pave research ideas.

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BC103-CELL AND MOLECULAR BIOLOGY

(Core 3)

SEM: I Lecture/Week: 6

BC103 Credits: 6

Objectives:

i. To have a basic understanding about the morphology of cell & cell organelles and its

function in detail.

ii. To learn the structure, function and molecular mechanism of the genetic material.

iii. Students could able to describe the general principles of gene organization and

expression in both prokaryotic and eukaryotic organisms.

iv. To learn how to interpret the outcome of experiments that involves the use of

recombinant DNA technology and other common gene analysis techniques.

v. To understand how to relate properties of cancerous cells to mutational changes in

gene function.

Unit - I

Cell Introduction: Structure and function prokaryotic and eukaryotic cells. Mechanism of

cell division – mitosis and meiosis, Structure and organization of chromatin. Structure and

function of cell membranes and organelles – mitochondria, chloroplasts (and their genetic

organization) endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes and their

functions. Membrane models, lipid assembly and membrane receptors. Intracellular

compartments, secretory and endocytic pathways in protein sorting, cytoskeleton, nucleus,

Membrane transport – active and passive transport. Microtubules and microfilaments. (https://www.diffen.com/difference/Eukaryotic_Cell_vs_Prokaryotic_Cell)

Unit - II

DNA Replication, Repair and Mutation: DNA in prokaryotes and eukaryotes. Mode of

replication; experimental findings of Meselson & Stahl. Enzymes involved in replication,

events on the replication fork and termination, mechanism of replication. Inhibitors of DNA

replication and DNA repair mechanisms (Direct repair, excision repair, mismatch repair,

recombination repair, SOS response, Eukaryotic repair system).Type of damages and

mutation – point mutation and frame shift mutation. Suppressor Gene mutation and

chromosomal aberration.(Blended mode of teaching)

Unit III:

Transcription: Organization of transcriptional unit – prokaryotes and eukaryotes. RNA

polymerases – structure and functions. Promoters, transcription factors, transcription

complex assembly and mechanism of transcription- Operon model. Transcriptional

regulation –hormonal (steroid hormone receptors), phosphorylation (STAT proteins),

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activation of transcriptional elongation by HIV tat protein. Post-transcriptional processing.

Alternative splicing. Catalytic RNA (ribozymes), antisense RNA. Inhibitors of transcription.

(https://www.atdbio.com/content/14/Transcription-Translation-and-Replication)

Unit - IV

Translation: The genetic code – specificity, redundancy and wobble hypothesis.

Mitochondrial and chloroplast genetic codons. Components of protein synthesis– mRNA,

rRNA and tRNA. Mechanism of protein synthesis. Regulation of protein synthesis -

constitutive and narrow domain regulation. Inhibition of protein synthesis. Co- and post-

translational modifications. Protein targeting- the signal sequence hypothesis, targeting

proteins to membranes, nucleus and intracellular organelles. Protein degradation - ubiquitin

pathway. Protein folding - models, molecular chaperones.

Unit - V

Gene expression and regulation: Levels of gene expression. Principles of gene regulation.

Upregulation, downregulation, induction and repression. Comparison of gene regulation

strategies in prokaryotes and eukaryotes. Genetic and epigenetic gene regulation by DNA

methylation. Methylation and gene regulation in mammals and plants. Epigenetic gene

regulation by DNA methylation in mammals - role of imprinting and X-chromosome

inactivation.(https://www2.le.ac.uk/projects/vgec/highereducation/topics/geneexpression-

Regulation)

Unit VI:

Cell Migration and its Control Mechanisms, Cell Migration and Neurite Outgrowth,

The Tumour Microenvironment: The Social Environment of the Cancer Cell.

Recommended Books:

1. Molecular Cell Biology, 5th edition, Harvey Lodish, Arnold Berk, Paul Matsudaira, chris

A. Kaiser, Monty Krieger, Mathew P Scott, Lawrence Zipursky, James Darnell, W.H

Freeman & Co. 2004, ISBN - 0716743663

2. Genes VIII, Benjamin Lewin, Pearson Prentice Hall, 2004, ISBN - 0131238264

3. Molecular Biology, David Friefelder, Jones & Bartlett Publishers ISBN 0867200693 (0-

86720-069-3).

4. Molecular Biology of The Cell, 4th edition, Bruce Alberts, Alexander Johnson, Julian

Lewis, Martin Raff, Keith Roberts, and Peter Walter, Garland edition, ISBN-10: 0-8153-

4072-9

5. Cell Biology and Histology, 6th edition, Gartner et al., Lippincott William and Wilkins

Publishers, ISBN - 1608313212.

6. Cell Biology and Molecular Biology, 8th edition, EDP De Robertis and EMF De Robertis,

Lippincott Williams and Wilkins, 2006, ISBN - 0781734932

7. Molecular Biology of the Gene, 6th edition, James D Watson, 2008, Cold Spring Harbor

Laboratory, ISBN 978-080539592-1

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8. Becker’s World of The Cell, 8th edition, Jerrf Hardin, Gregory Bertoni, Lewis Kleinsmith,

2011, Pearson Publications, ISBN - 0321709780

9. Cell and Molecular Biology Concepts & Experiments, 5th edition, Gerald Karp, 2008,

wiley Publications, ISBN - 978-0-470-04214-4

COURSE OUTCOME:

i) To have a basic understanding about the morphology of cell & cell organelles and its

function in detail.

ii) To understand the structure, function and molecular mechanism of the genetic

material.

iii) "Students could able to describe the general principles of gene organization and

expression in both prokaryotic and eukaryotic organisms."

iv) To learn how to Interpret the outcome of experiments that involve the use of

recombinant DNA technology and other common gene analysis techniques

v) To understand how to relate properties of cancerous cells to mutational changes in

gene function.

vi) Understand receptor subclasses and their possible uses in cell signalling.

vii) students understand the mechanisms by which different messenger-receptor

interactions bring about long or short-term changes in cell state.

viii) Students can make the Knowledge of the relationship between structure and function

at organ and/or organism level, of important cell biological communication principles

and processes, and how they are regulated.

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BC104 - BIOCHEMICAL TECHNIQUES

(Core 4)

SEM: I Lecture/Week: 6

BC104 Credits: 6

Objectives:

i. This course will introduce some of the experimental techniques used in

biochemistry and molecular biology

ii. Students can able to learn methods for purifying proteins, expressing

recombinant proteins in bacterial cells, and analyzing biological molecules by

electrophoresis, Western blotting, and enzyme activity assays.

iii. To be able to communicate and discuss General principles of biochemical

investigation

iv. To perceive the strengths, limitations and creative use of techniques for

problem-solving

v. Familiarity with working principles, tools and techniques of analytical

techniques

Unit - I

Units of measurement of solutes in solution : Normality, Molarity, molality and

milliosmol. Ionic strength.pH, pOH, Henderson – Hesselbalch equation, buffers, pH of body

fluids. Measurement of pH by indicators, Zwitter ions.pH dependent ionization of amino

acids and proteins. Colloids and their application, Viscosity, surface tension and Donnan

membrane equilibrium.Principles of electrochemical techniques – measurement of pH by

glass electrode and hydrogen electrode.Oxygen electrode – principles, operation of a Clarke

electrode and its applications.(Blended mode of teaching)

Unit - II

Cell Fractionation Techniques : Cell lysis, differential and density gradient centrifugation,

Salting in, Salting out, Dialysis, Ultrafiltration. Ultra Centrifugation - preparative and

analytical ultracentrifuge, Svedberg's constant, Sedimentation velocity and Sedimentation

equilibrium, Schleiran optics. Chromatographic Techniques - Principles and Applications of

Paper, TLC, Adsorption, Ion exchanges, Gel filtration, Affinity, GLC, Chromato focusing,

HPLC,FPLC.( https://study.com/academy/lesson/cell-fractionation-definition)-

Unit - III

Electrophoretic Techniques: Polyacrylamide gel electrophoresis, SDS-PAGE, 2D –

PAGE, Isoelectric focusing, Visualizing protein bands – CBB & Silver staining. Agarose

gel Electrophoresis, pulse field electrophoresis, high voltage electrophoresis, Capillary

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Electrophoresis, Isotachophoresis, RFLP, FISH. Blotting techniques and its applications –

Western, Northern & Southern.

Unit - IV

Isotopic Tracers: Heavy isotopes and radio isotopes theory. Application of radio isotopes in

Biology - 3H, 14C, 32P, 131I, 35S, concept of half-life, decay constant, detection and

quantitation - GM counter and scintillation counter, solid and liquid scintillation. Quenching

and quench correction, Cerenkov counting. Specific activity, carrier free isotope, isotope

dilution techniques and autoradiography.Radiation hazards and radio dosimetry.

Unit - V

Spectroscopic techniques: colorimetry, spectrophotometry – UV & visible, Principle –

Beer & Lambert’s law, Extinction coefficient. Principle and application - Atomic absorption

spectroscopy, Fluorimetry.Basic principle and application of mass spectra, NMR, ESR, ESI-

MS, MALDI-TOF, CD, MRI, CTscans.Biochips (DNA chips, Protein chips and Sensor

chips).Vibration Spectra – IR and Raman – Principles and Applications.X-ray

crystallography – protein crystals, Bragg’s law.(Blended mode of teaching*)

Unit VI:

Hydrodynamic methods of separation of biomolecules such as viscosity and

sedimentation- their principles, variants and applications. Hydrodynamic voltammetr and its

principle and application.

Recommended Books:

1. Wilson and Walker. A biologists guide to principles and techniques of practical

biochemistry. 5th ed. Cambridge University Press 2000.

2. Boyer, R. Modern Experimental Biochemistry. 3rd ed. Addison Weslery Longman,

2000.

3. Upadhyay, Upadhyay and Nath. Biophysical Chemistry Principles and Techniques.

Himalaya Publ. 1997.

4. Simpson CFA &Whittacker, M. Electrophoretic techniques.

5. Sambrook. Molecular Cloning. Cold Spring Harbor Laboratory, 2001.

6. Friefelder and Friefelder. Physical Biochemistry – Applications to Biochemistry and

Molecular Biology. WH Freeman & Co. 1994.

7. Pavia et al. Introduction to Spectroscopy. 3rd ed. Brooks/Cole Pub Co., 2000.

COURSE OUTCOMES:

i) This course will introduce some of the experimental techniques used in biochemistry

and molecular biology

ii) Students can able to learn methods for purifying proteins, expressing recombinant

proteins in bacterial cells, and analyzing biological molecules by electrophoresis,

Western blotting, and enzyme activity assays.

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iii) To be able to communicate and discuss General principles of biochemical

investigation

iv) To understand the strengths, limitations and creative use of techniques for problem-

solving

v) Familiarity with working principles, tools and techniques of analytical techniques

vi) To be able to organize the lab results and write a report on a standard paper format

vii) Students can understand the knowledge for the separation of proteins/peptides by

selecting appropriate separation techniques.

viii) Students can able to Characterize certain functionalities of biomolecules by using

spectroscopic technique

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BC105 Lab Course – I

(Core 5)

SEM: I Lecture/Week: 6

BC105 Credits: 4

Objectives

i. Students will develop the habit of being cautious, safe and will learn to follow basic

laboratory rules.

ii. Students will be able to design a experiment and learn to trouble shoot.

iii. The course helps to understand the principles of Instrumentation and promote

working ability

iv. Students will have intense working knowledge on basic scientific equipment and to

analyze the data.

v. Students will have the exposure to perform the experiments individually.

1. Calculation and preparation of standard solution

2. Preparation of buffer, training to use of balance and PH meter

3. Determine pKa and pI of acidic, basic, and neutral amino acid

4. Estimation of amino acids by Ninhydrin methods

5. Estimation of reducing sugar by DNSA method

6. Estimation of protein by Lowry’s method

7. Estimation of DNA by Diphenylamine method

8. Estimation of RNA by Orcinol method

9. Estimation of inorganic phosphorous by Fiske and Subbarow method

10. Determination of calcium in milk by Titration method

11. Separation of purines and pyrimidines by paper chromatography

12. Separation of phospholipids by thin layer chromatography

13. Separation of amino acids by ion exchange chromatography

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COURSE OUTCOME:

i) Students will develop the habit of being cautious, safe and will learn to follow basic

laboratory rules.

ii) Students will be able to design a experiment and learn to troubleshoot.

iii) The course helps to understand the principles of Instrumentation and promote working

ability.

iv) Students will have intense working knowledge on basic scientific equipment and to

analyze the data.

v) Students will have the exposure to perform the experiments individually.

vi) Students will know to handle the chemicals practically safe and work based on the

prescribed protocols.

vii) Laboratory studies can create a learning environment that encourages students to

question, thereby fostering critical thinking.

viii) Students will gain conceptual understanding of subject matter, scientific reasoning

skills, laboratory manipulative skills.

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BC 201 - BIOCHEMISTRY OF SIGNAL TRANSDUCTION AND REGULATION

(Core 6)

SEM: II Lecture/Week: 6

BC201 Credits: 6

Objectives

i. Helps to distinguish the key principles of biochemical metabolic concepts

ii. Students will learn the signalling pathways that will help them in further studies.

iii. Students grasp the basic need of the signalling molecules and the consequesnce on

their absence.

iv. Students will be exposed to most of the actions of the biological system,which they

will study in depth with signalling molecules.

v. Students can able to understand the function of specific anabolic and catabolic

pathways and how these pathways are controlled and interrelated

Unit - I

Regulation of transcription and translation in prokaryotes: Positive and negative

control, repressor and inducer, concept of operon, lac-, and trp operons, attenuation,

regulons. Regulation in eukaryotes- gene families, regulatory strategies in eukaryotes, gene

alteration, regulation of synthesis of primary transcripts, hormonal control, transcription

factors, transcription factors: targets of signaling pathways, DNA binding motifs in pro- and

eukaryotes, Helix turn, helix, zinc fingers, leucine zippers/ b zip, helix loop helix motifs.

Regulation at the level of translation in prokaryotes and eukaryotes.

(vbio.weebly.com/uploads/.../15.2_-_regulation_of_transcription_and_translation.pptx*)

Unit- II

Signal transduction: definition, signals, ligands and receptors. Endocrine, paracrine and

autocrine signaling. Sensory Transduction : Nerve impulse transmission – Nerve cells,

synapses, reflex arc structure, Resting membrane potential, action potential, voltage gated

ion-channels, impulse transmission, neurotransmitters, neurotransmitter receptors. Rod and

cone cells in the retina, biochemical changes in the visual cycle, photochemical reaction and

regulation of rhodopsin. Odor receptors. Chemistry of muscle contraction – actin and

myosin filaments, theories involved in muscle contraction, mechanism of muscle

contraction, energy sources for muscle contraction.(Chalk and talk*)

Unit - III

Receptors and signaling pathways: cell signaling, cell surface receptors. G Protein coupled

receptors- structure, mechanism of signal transmission, regulatory GTPases, heterotrimeric

G proteins and effector molecules of G Proteins. Receptor tyrosine kinases, Role of

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phosphotyrosine in SH2 domain binding. Signal transmission via Ras proteins and MAP

kinase pathways. Signaling molecules- cAMP, cGMP, metabolic pathways for the formation

of inositol triphosphate from phosphatidyl inositol diphosphate, Ca2+, DAG and NO as

signaling molecules, ryanodine and other Ca2+ receptors, phosphoregulation of inositol and

the calcium channel activation. Ser/Thr-specific protein kinases and phosphatases.

Unit - IV

Signaling by nuclear receptors: ligands, structure and functions of nuclear receptors,

nuclear functions for hormones/metabolites - orphan receptors; cytoplasmic functions and

crosstalk with signaling molecules, signaling pathway of the steroid hormone receptors.

Cytokine receptors- structure and activation of cytokine receptors, Jak-Stat path way, Janus

kinases, Stat proteins.

Unit - V

Regulation of the cell cycle: Overview of the cell cycle, cell cycle control mechanisms,

Cyclin-dependent protein kinases (CDKs), regulation of cell cycle by proteolysis, G1/S

Phase transition, G2/M Phase transition, cell cycle control of DNA replication, DNA damage

check points. Cancer, types of cancer, factors causing cancer-physical, chemical and

biological agents. Errors in function of signal proteins and tumerogenesis.Oncogenes, proto-

oncogenes and tumor suppressor genes.Tumor suppressor protein p53 and its role in tumor

suppression.Tumor suppressor APC and Wnt/-Catenin signaling

( www.wormbook.org/chapters/www_cellcyclereguln/cellcyclereguln.html)

Unit VI:

Signal transduction in Health and Disease: Cancer, Neurodegeneration, Diabetes and

Obesity and Inflammation

Recommended Books:

1) Molecular biology- David Freifelder, Narosa Publishing House Pvt. Limited, 2005

2) Biochemistry of Signal Transduction and Regulation. 3rd Edition. Gerhard Krauss,

2003 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 3-527-30591-2

3) Molecular Biology of the Cell, 4th edition, Bruce Alberts. New York: Garland

Science; 2002. ISBN-10: 0-8153-3218-1ISBN-10: 0-8153-4072-9

4) Molecular Cell Biology, 4th edition, Harvey Lodish.New York: W. H. Freeman;

2000. ISBN-10: 0-7167-3136-3

5) Principles of cell and molecular biology- Lewis Kleinsmith, 2nd edition, illustrated,

HarperCollins, 1995.

COURSE OUTCOME:

i) Help understand the key principles of biochemical metabolic concepts

ii) Students will learn the signalling pathways that will help them in further studies.

iii) Students learn the basic need of the signalling molecules and the consequesnce on

their absence.

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iv) Students will be exposed to most of the actions of the biological system,which they

will study in depth with signalling molecules.

v) Students can able to understand the function of specific anabolic and catabolic

pathways and how these pathways are controlled and interrelated

vi) How current research has provided us with an understanding of the molecular basis of

the control of metabolism

vii) "How to communicate scientific information effectively in writing Hypothesis-based

experimental design"

viii) The course aims to give participants a basic knowledge of mechanisms of signal

transduction and the significance of signal transduction in physiology and

pathophysiology.

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BC 202 - INTERMEDIARY METABOLISM

(Core 7)

SEM: II Lecture/Week: 6

BC202 Credits: 6

Objectives

i. To learn the metabolism and integration of biomolecules that takes place in human

system.

ii. Integrate the various aspects of metabolism & their regulatory pathways

iii. Students can understand the fundamental energetics of biochemical processes

iv. To elaborate the relation between biochemical defects and metabolic disorders.

v. To follow the organization of signaling pathways.

Unit - I

Introduction - Overview of major classes of biomolecules, forces stabilizing biomolecules.

General scheme of metabolism, historical and experimental details in derivation of a

metabolic pathway, catabolic, anabolic and amphibolic pathways. Thermodynamics and

metabolism: Cell bioenergetics, laws of thermodynamics, standard free energy, enthalpy,

entropy. Exergonic and endergonic reactions.Definiton of open, closed and isolated system –

Oxidative phosphorylation. Electron transport chain. Standard free energy change of a

chemical reaction, redox potentials, ATP and high energy phosphate compounds.(Blended

Mode of teaching)

Unit - II

Carbohydrates metabolism : Glycolysis and gluconeogenesis – pathway, key enzymes and

co-ordinate regulation.The citric acid cycle and its regulation.The pentose phosphate

pathway.Metabolism of glycogen and regulation.Key junctions in metabolism– glucose-6-

phosphate, pyruvate and acetyl CoA.Blood glucose homeostasis– role of tissues and

hormones.(chalk and talk)

Unit - III

Amino acid metabolism: biosynthesis and degradation of amino acids and their regulation.

Transamination and deamination, ammonia formation, the urea cycle and regulation of

ureogenesis.

Unit IV

Lipids metabolism : Lipogenesis: biosynthesis of fatty acid, triglycerides, phospholipids,

and cholesterol. Regulation of triacylglycerol, phospholipids and cholesterol

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biosynthesis.Oxidation of lipids.Role of carnitine cycle in the regulation of β -oxidation.

Ketogenesis and its control.Lipoprotein metabolism - exogenous and endogenus pathways.

Unit - V

Nucleic acid metabolism- biosynthesis and catabolism of purines and pyrimidines and their

regulation.( https://www.slideshare.net/senchiy/nucleic-acids-and-nucleotide)

Unit VI:

Bioenergies in metabolism: High energy phosphates. Components of Electron Transport

chain and the sequence of electron transport. Mechanism of ATP synthesis; Oxidative

phosphorylation – the chemiosmotic theory. Uncoupling of oxidative phosphorylation.

Inhibitors of respiratory chain and oxidative phosphorylation. Mitochondrial transport

systems, ATP/ADP exchange, malate/glycerol phosphate shuttle.

Recommended Books:

7) Biochemistry – L. Stryer.

8) Principles of Biochemistry – R. Horton et al.

9) Lehninger’s Principles of Biochemistry - D. L. Nelson and M. M. Cox.

10) Harpers Biochemistry- R. K. Murray et al.

11) Principles of Biochemistry- G. L. Zubay.

12) Outlines of biochemistry- Lippincott.

COURSE OUTCOME:

i) To learn the metabolism and integration of biomolecules that takes place in human

system.

ii) Integrate the various aspects of metabolism & their regulatory pathways

iii) Students can understand the fundamental energetics of biochemical processes

iv) To understand the relation between biochemical defects and metabolic

disorders.

v) To understand the organization of signaling pathways.

vi) To understand the role of membrane processes in metabolism

vii) Overall, gaining an understanding of the processes of metabolic transformation at the

molecular level and how these processes are studied.

viii) Afford students opportunity to appreciate the relevance/applications of biochemistry in

our daily activities.

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Elective Paper – I

BC203 - ECOLOGY AND ENVIRONMENTAL BIOLOGY

(Elective 1)

SEM: II Lecture/Week: 5

BC203 Credits: 3

Objectives

i. To study the physical and biological characters of the environment and the inter-

relationship between biotic and abiotic components of nature as well as

relationship among the individuals of the biotic components.

ii. To understanding of current environmental issues and how global problems affect us

locally

iii. Describe the ecological and evolutionary influence of abiotic factors on organisms

and how these factors affect the distribution and abundance of species.

iv. To understand the core ecological principles, and define scientific principles and

concepts as related to environmental studies and sustainability

v. Students should be able to demonstrate an

vi. Understanding of environmental interrelationships and of contemporary

environmental issues.

Unit - I

The Environment: definition, types of environment and their importance: physical

environment; biotic environment; social environment; biotic and abiotic interactions.

Ecology: scope of ecology; historical background; ecology in India; terminology of ecology;

basic concepts of ecology.(Blended mode of teaching)

Unit - II

Environmental Complex: Environmental and ecological factors-Direct and indirect factors;

four categories of ecological factors-climatic, topographic, edaphic and biotic factors;

interaction of ecological factors. Species Interactions: Types of interactions, interspecific

competition, herbivory, carnivory, pollination, symbiosis. Habitat and Niche: Concept of

habitat and niche; niche width and overlap; fundamental and realized niche; resource

partitioning; character displacement.

Unit - III

Population Ecology: Characteristics of a population; population growth curves; population

regulation; life history strategies (r and K selection); concept of metapopulation – demes and

dispersal, interdemic extinctions, age structured populations. Community Ecology: Nature of

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communities; community structure and attributes; levels of species diversity and its

measurement; edges and ecotones. Ecological Succession: Types; mechanisms; changes

involved in succession; concept of climax.

Unit - IV

Ecosystem Ecology: Ecosystem structure; ecosystem function; energy flow and mineral

cycling (C, N, and P); primary production and decomposition; structure and function of

some Indian ecosystems: terrestrial (forest, grassland) and aquatic (fresh water, marine,

eustarine). Biogeography: Major terrestrial biomes; theory of island biogeography;

biogeographical zones of India.(Chalk an talk)

Unit - V

Applied Ecology: Environmental pollution; global environmental change; biodiversity:

status, monitoring and documentation; major drivers of biodiversity change; biodiversity

management approaches. Conservation Biology: Principles of conservation, major

approaches to management, Indian case studies on conservation/management strategy

(Project Tiger, Biosphere reserves).

Unit VI:

Waste Management: Sources, generation, classification & composition of solid wastes. Solid

waste management methods - Sanitary land filling, Recycling, Composting, Vermi-

composting, Incineration, energy recovery from organic waste. Hospital Waste

Management, Hazardous Waste Management & Handling rules, 1989 & 2000

(amendments).( www.businessdictionary.com/definition/waste-management.html)

Recommended Books:

1. Ecology and Environment - PD. Sharma, Rastogi Publications, 7th edition (2007).

2. Ecology-from individuals to ecosystems – Michael Begon, Colin R, Townsend and

John L Harper, Blackwell publishing - 4th edition (2006)

3. Ecology-the plants, animals and the environment-Michael Allaby, Facts on file 1st

edition (2009)

4. Ecology-Robert E Ricklefs, W.H.Freeman Publisher, Fourth edition (2000)

COURSE OUTCOME:

1. To study the physical and biological characters of the environment and the

inter-relationship between biotic and abiotic components of nature as well as

relationship among the individuals of the biotic components

2. To understanding of current environmental issues and how global problems

affect us locally.

3. Describe the ecological and evolutionary influence of abiotic factors on

organisms and how these factors affect the distribution and abundance of

species.

4. To understanding of core ecological principles, and define scientific

principles and concepts as related to environmental studies and sustainability.

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5. Students should be able to demonstrate an understanding of environmental

interrelationships and of contemporary environmental issues.

6. To study the extinct species and the cause related to it.

7. Students will able to differentiate the past world environment with the present

and will think on evolution.

8. Students will learn at the end of the course to conserve the nature and will be

able to develop new strategies to preserve the sources of life.

BC204 - LABORATORY COURSE II

(Core 8)

SEM: II Lecture/Week: 6

BC204 Credits: 6

Objectives

i. Extract gene sequence data from public databases, apply principles of gene structure

and expression to identify features within gene sequence, and analyze gene

sequence manually using online software tools

ii. Interpret and discuss the outcome of experiments formally through oral presentations

and written reports

iii. independently clone any gene into a plasmid vector (from RNA extraction, reverse

transcription, polymerase chain reaction, ligation, bacterial transformation, to DNA

extraction, DNA mapping and primer design)

iv. transfect plasmids and silencing RNAs to over-express or knock down protein

expression in a primary cell line, extract protein, assess and quantify expression

using Western blotting

v. Students learn to handle all the equipment regularly that used in DNA manipulation,

including balances, pipettes, electrophoresis and centrifuges and thereby obtain

basic laboratory skills.

1. Cell culture equipment and safety

2. Sterile and Aseptic techniques

3. Cell line repository

4. Preparation of Media for Animal Cell Culture

5. Plating cells from frozen stock

6. Sub culturing adherent Animal cells in culture

7. Cryopreservation and Storage of Animal Cells

8. Determination of Contamination in culture lab and cells

9. Counting cells using a hemocytometer

10. Assessment of Cytotoxicity assay

11. Estimation of total RNA and cDNA synthesis

12. Reverse transcriptase Polymerase chain reaction

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COURSE OUTCOME:

1. Extract gene sequence data from public databases, apply principles of gene structure and

expression to identify features within gene sequence, and analyze gene sequence manually

using online software tools.

2. Interpret and discuss the outcome of experiments formally through oral presentations and

written reports.

3. Independently clone any gene into a plasmid vector (from RNA extraction, reverse

transcription, polymerase chain reaction, ligation, bacterial transformation, to DNA

extraction, DNA mapping and primer design).

4. Transfect plasmids and silencing RNAs to over-express or knock down protein expression

in a primary cell line, extract protein, assess and quantify expression using Western blotting.

5. Students learn to handle all the equipment regularly that used in DNA manipulation,

including balances, pipettes, electrophoresis and centrifuges and thereby obtain basic

laboratory skills.

6. To obtain basic laboratory skills such as microscopy, spectrophotometry, measuring, etc.

7. The ability to apply lecture concepts in a laboratory setting.

8. The ability to write scientific reports including analysis of data and graphing.

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BC2ED - GENETICS (ED PAPER)

(Non Major Elective I)

SEM: II Lecture/Week: 3

BC2ED Credits: 2

Objectives

i. Identify and describe the process and purposes of the cell cycle, meiosis, and mitosis,

as well as predict the outcomes of these processes.

ii. Transmission genetics problems, make accurate predictions about inheritance of

genetic traits, and map the locations of genes

iii. To identify the parts, structure, and dimensions of DNA molecules, RNA molecules,

and chromosomes, and be able to categorize DNA as well as describe how DNA

is stored

iv. To describe what causes and consequences of DNA sequence changes and how cells

prevent these changes, as well as make predictions about the causes and effects

of changes in DNA

v. To describe applications and techniques of modern genetic technology, as well as

select the correct techniques to solve practical genetic problems

Unit - I

Introduction to Genetics: Brief history/basic concepts of genetics, Cell division and

chromosomes. Mendelian genetics/monohybrid, dihybrid cross. Mendelian

genetics/trihybrid cross, probability. Modification of Mendelian ratios/incomplete and

codominance.Modification of Mendelian ratios/incomplete and codominance.Structure of

Gene - Interaction of Gene - Commentary Factors, Supplementary Factors, Inhibitory and

Lethal Factors - Atavism. (https://www.slideshare.net/vanessaceline/intorduction-to-

genetics)

Unit - II

Diploid chromosomes number- Sex differentiation and sex determination.The X

chromosomes, Barr bodies, the Lyon hypothesis. Aneuploidy and polyploidy: Gene deletion,

duplication, inversions and translocation. Sex Linkage in Drosopohila and Man, Sex

Influenced and Sex Limited Genes - Non-Disjunction and Gynandromorphs - Cytoplasmic

Inheritance - Maternal Effect OnLimnaea (Shell Coiling), Male Sterility (Rode's

Experiment).CO2 sensitivity In Drosophila, Kappa particles in Paramecium, Milk Factor in

Mice.(Blended mode of teaching)

Unit- III

Blood Groups and their Inheritance in Human - Linkage and Crossing Over:- Drosophila -

Morgans' Experiments - Complete and Incomplete Linkage, Linkage Groups, Crossing Over

types, Mechanisms - Cytological Evidence for Crossing Over, Mapping of Chromosomes -

Interference and Coincidence.

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Unit IV:

Nature and Function of Genetic Material - Fine Structure of the Gene - Cistron, Recon,

Muton - Mutation - Molecular Basis of Mutation, Types of Mutation, Mutagens, Mutable

and Mutator Genes. Chromosomal Aberrations - Numerical and Structural Examples from

Human.

Unit V:

Applied Genetics – Animal Breeding - Heterosis, Inbreeding, Out Breeding, Out Crossing,

Hybrid Vigour. Population Genetics, Evolutionary genetics, Hardy Weinberg Law - Gene

Frequency, Factors Affecting Gene Frequency, Eugenics, Euphenics and Euthenics,

Bioethics. (www.goldiesroom.org/...)

Unit VI:

Genetic Principles and their application in medical practice; Case studies (Interacting with

patients, learning family history and drawing pedigree chart); Syndromes and disorders:

definition and their genetic basis - Cystic fibrosis and Tay Sach’s Syndrome;

Phenylketonuria and Galactosemia; Ethical issues with clinical genetics.

Recommended Books:

1. Genetics by Verma, P.S. and V. K.Aggarwal.

2. Genetics by Russell P.J.

3. Genetics analysis and principles by Brooker R.J and McGraw Hill.

4. Basic Genetics my Miglani G.S.

5. Genetics: Analysis of genes and genomes by Hartl D.L and Jones E.W.

COURSE OUTCOME:

1.Identify and describe the process and purposes of the cell cycle, meiosis, and

mitosis, as well as predict the outcomes of these processes.

2.Transmission genetics problems, make accurate predictions about inheritance of

genetic traits, and map the locations of genes.

3.To identify the parts, structure, and dimensions of DNA molecules, RNA

molecules, and chromosomes, and be able to categorize DNA as well as describe how DNA

is stored.

4.To describe what causes and consequences of DNA sequence changes and how

cells prevent these changes, as well as make predictions about the causes and effects of

changes in DNA.

5.To describe applications and techniques of modern genetic technology, as well as

select the correct techniques to solve practical genetic problems.

6.To carry out genetics laboratory and field research techniques.

7.To describe experimental results in written format both informally and in formal

manuscript format.

8.To accurately diagram and describe the processes of replication, transcription,

translation, as well as predict the outcomes of these processes"

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BC301-IMMUNOLOGY

(Core 9)

SEM: III Lecture/Week: 6

BC301 Credits: 6

Objectives

i. Describe the basic mechanisms, distinctions and functional interplay of innate and

adaptive immunity

ii. Define the cellular/molecular pathways of humoral/cell-mediated adaptive responses

iii. Define the basic mechanisms that regulate immune responses and maintain tolerance

iv. To demonstrate the molecular basis of complex, cellular processes involved in

inflammation and immunity, in states of health and disease.

v. Describe basic and state-of-the-art experimental methods and technologies

Unit - I

Historical perspective: contribution by metchinikoff, Edward Jenner, Louis Pasteur and

Wu and Kabat. Types of immunity – innate and acquired. Humoral and cell mediated

immunity. Central and peripheral lymphoid organs – Thymus, bone marrow, spleen, lymph

nodes and other peripheral lymphoid tissues – MALT, GALT and CALT. Cells of the

immune system- lymphocytes, mononuclear phagocytes – dendritic cells, granulocytes, NK

cells and mast cells.Immunoglobulins – structure, classification and functions. Idiotype

network hypothesis. Antigen, types of antigen, antigen Vsimmunogens, Haptens. Factors

influencing immunogenicity.Isotypes, allotypes and idiotypes.(Blended mode of teaching)

Unit - II

Complement system: components of complement activation and its biological consequences

– classical, alternative and lectin pathways. Clonal selection theory.Organization and

expression of immunoglobulin genes, generation of antibody diversity.Class switching.

Overview of B cell & T cell, types of immune response, T – cell, B- cell receptors, Antigen

recognition – processing and presentation to T- cells. Interaction of T and B cells.Effector

mechanisms – macrophage activation. Cell mediated cytotoxicity, Cytokines types,

regulation of immune response : immune tolerance and immunosuppression.(Chalk and

talk)

Unit - III

Major Histocompatibility complex (MHC): MHC genes and products. Polymorphism of

MHC genes, role of MHC antigen in immune response, MHC antigens in transplantation.

Transplantation types, allograft rejection mechanism. Immune response to infectious

diseases – Viral, bacterial and protozoal.AIDS and other immunodeficiency disorders.

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Autoimmunity: Mechanism of induction of organ specific and systemic auto immune

diseases. Hypersensitivity – types. Immune response to cancer, immunotherapy.

Unit IV

Immunization practices – active and passive immunization. Vaccines – killed, attenuated –

toxoids. Recombinant vector vaccines – DNA vaccines, synthetic peptide vaccines – anti

idiotype vaccines.Humanized antibodies and plantibodies.Production of polyclonal and

monoclonal antibodies.Principles, techniques and application.Genetically engineered

antibodies.Abzymes.

Unit V

Immunotechniques: Agglutination and precipitation technique. Immuno – electrophoresis,

RIA, immunoblotting, Avidin – biotin mediated immune assay. Immunohistochemistry –

immunofluorescence, immune ferritin technique. Fluorescent immunoassay, fluorescence

activated cell sorting (FACS). Cytokines assay: ELISA and ELISPOT. Lymphocytes

transformation test (LTT); Lymphoblastoid cell lines. Experimental animal models: inbred

strains, SCID mice, nude mice, knockout mice fully cloned animals.

(www.biologydiscussion.com/biochemistry/immunochemical...)

Unit VI:

Recent studies on Auto-immune disorders, Hypersensitivity. Dynamics of the

immune response. The immune response in health and disease.

Recommended Books:

1. Geoffrey Zubay - (1972), Immunology, 4thedition, W.M.C. Brown publishers.

2. Janis Kuby - (1997), immunology, 3rdedition, W.H. Freedom & co (Sd).

3. Kenneth M. Murphy, Paul Travers, Mark Walport - (2007),

Janeway’simmunobiology, 7thedition, Garland Science.

4. Peter Delves, Seamus Martin, Dennis Burton, Ivan Roitt - (2006),Roitt's

EssentialImmunology, 11th edition, Wiley-Blackwell.

5. Abul K. Abbas, Andrew H. Lichtman, Jordan S. Pober - (1994), Cellular and

molecular immunology, 2ndedition, B. Saunders Company.

6. Donald Mackay Weir & Stewart John - (1997), Immunology, 8th edition, Churchill

Livingstone.

COURSE OUTCOME

1. Describe the basic mechanisms, distinctions and functional interplay of innate

and adaptive immunity.

2. Define the cellular/molecular pathways of humoral/cell-mediated adaptive

responses.

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3. Define the basic mechanisms that regulate immune responses and maintain

tolerance.

4. Understand the molecular basis of complex, cellular processes involved in

inflammation and immunity, in states of health and disease .

5. Describe basic and state-of-the-art experimental methods and technologies .

6. Integrate knowledge of each subsystem to see their contribution to the

functioning of higher-level systems in health and disease.

7. Apply understanding of basic and state-of-the-art experimental methods and

technologies in the design of research plan to test specific hypotheses.

8. Translate understanding of basic mechanisms into identification of biological,

clinical and therapeutic implications.

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BC302 - GENETIC ENGINEERING AND MOLECULAR

TECHNIQUES

(Core 10)

SEM: III Lecture/Week: 6

BC201 Credits: 6

Objectives

i. This course is to discipline to students knowledge of main engines of implementation

and transmission of a genetic material at molecular and cellular levels

ii. The methods of change of a genetic material and constructioning of transgene

organisms with the given properties.

iii. Students can be understand Know the natural function of restriction endonucleases

and how a normal bacterial cell protects its DNA from their activity

iv. Understand the value of and the processes involved with the polymerase chain

reaction (PCR).

v. To understand the function of creative use of modern tools and techniques for

manipulation and analysis of genomic sequences

Unit - I

Introduction to gene cloning: Restriction and modification enzymes. Cloning vectors:

Characteristics, Natural & artificial plasmids as vectors - advantages and disadvantages.

Vectors used for cloning in E.coli., yeast, higher plants (Ti plasmid derivatives,

caulimovirus) and animal cells (constructs of SV 40 and retroviruses). Characteristics of

expression vectors. Construction of DNA libraries - genomic and cDNA libraries. Screening

of recombinants.(Blended of teaching)

Unit - II

Transposons and transposable elements: Transgenic animals - Gene transfer methods in

animals. Recombinant selection and screening. Totipotency, haploids, growth of animal cell

lines. Competent cells preparation, electroporation, microinjection and particle

bombardment method, and selection of transformants. Transgenic plants - Use of

agrobacterium for genetic engineering in plants. Plant cell cultures for the production of

important compounds. Plant tissue culture – Micropropagation, protoplast isolation, somatic

hybrids. Identification of transformed cells into callus and regeneration of transgenic plants

Unit - III

Molecular techniques: Polymerase chain reaction – principle, types and applications.

Sanger’s and Maxam-Gilbert’s method for DNA sequencing. DNA Finger Printing - RAPD,

RACE (Rapid Amplification of cDNA Ends), RFLP and AFLP analysis and its application

in forensic science, pedigree analysis, biodiversity, genetic counselling and germplasm

maintenance. DNA foot printing. Chromosome walking, chromosome jumping.

Mutagenicity test – Ames test. Markers linked to drug and disease resistant genes. Antisense

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technology and its application. Microarray technology: genomic and cDNA arrays.(

https://www.slideshare.net/drmalathi13/molecular-techniques)

Unit- IV

Gene therapy: Ex-vivo, Invivo, Insitu gene therapy Stratagies of gene therapy: Gene

augmentation – ADA defeiciency, CFTR, Antisense therapy, Ribozymes, Protein Aptamers,

Intrabodies. Stem cell therapy - Embryonic and adullt Stem Cells, Totipotent, Pluripotent

and Mulltipotent Cells. Testing and generation of embryonic stem cells, Testing for adult

stem cells and differentiation, Potential use of stem cells – Cell based therapies.

Unit –V

Human genome projects, gene bank. Genetically modified organisms (GMOs) in developed

and developing countries. Genetically modified foods – benefits and risks. Bioethics: Laws

and regulations in biotechnology, patent laws, and Intellectual property rights (IPR).

Biosafety, types of biosafety, advantage and disadvantage.Ethics in cloning and stem cell

research.

Unit VI:

Genetics of Metamorphosis, Regeneration & Aging – Compensatory regeneration in the Mammalian

Liver, Causes of Aging, Genetically regulated pathway of Aging. (chalk and talk)

Recommended Books:

1. Molecular Cloning: A Laboratory manual, J. Sambrook, E.Ffrisch and T. Maniatis,

Old Spring Harbor Laboratory Press New York, 2000

2. DNA Cloning : a Practical Approach, DM Glover and BD Hames, IRL Press

3. Molecular and Cellular methods in Biology and Medicine. PB Kaufman,W.Wu.D

Kim and LJ Cseke, CRC

4. DNA Science. A first Course in Recombinant Technology, DA Mickloss and GA

Freyer, Cold Spring Harbor Laboratory Press, New York 1990

5. Molecular Biotechnology (2nd Edn) SB Primrose, Blackwell Scietific Pub. Oxford,

1994

6. Milestones in Biotechnology. Classic papers on Genetic Engineering. JA Davies and

WS Reznikoff, Butterworth-Heinemann, Boston, 1992

7. Route Maps in Gene Technology, MR Walker and R Rapley, Blackwell Science Ltd,

Oxford 1997

8. Molecular Biotechnology. Glick

9. Principles of Gene Manipulation by Old and Primrose, Blackwell publications

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COURSE OUTCOME

1. This course is to discipline to student’s knowledge of main engines of

implementation and transmission of a genetic material at molecular and cellular

levels.

2. The methods of change of a genetic material and constructing of transgene organisms

with the given properties.

3. Students can be understood Know the natural function of restriction endonucleases

and how a normal bacterial cell protects its DNA from their activity.

4. Understand the value of and the processes involved with the polymerase chain

reaction (PCR).

5. To understand the function of creative use of modern tools and techniques for

manipulation and analysis of genomic sequences.

6. This technique can use to train students in strategizing research methodologies

employing genetic engineering techniques.

7. Understand the similarities and differences between how genetic information is

passed on in eukaryotes and prokaryotes.

8. Students can observe the Identify the fundamental differences between genetically

engineered crops and non-genetically engineered crops.

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BC303 - CLINICAL BIOCHEMSITRY

(Elective 2)

SEM: III Lecture/Week: 5

BC303 Credits: 3

Objectives

i. An advanced understanding and applied knowledge of the theory and practice of

clinical biochemistry;

ii. The student will be able to describe the structure, function and metabolic pathways

for carbohydrates, amino acids and lipids.

iii. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of

diabetes.

iv. To make the students biochemistry of membranes including chemical composition

and structure of biological membranes, as well as drug transporters

v. To impart thorough knowledge about the biochemical basis of various diseases and

disorders

Unit- I

Introduction to Biochemical laboratory: Roles of biochemical laboratory. Mechanization

and amomation in clinical biochemistry. Quality control in clinical laboratories. Total

laboratory uncertainty. Accuracy and precision. Selection and optimization of laboratory

methods, Clinical evaluvation of laboratory methods.

Biochemical analysis in urine. Clinical biochemical analysis of proteins. Plasma protein

spectrum during inflammation, paraproteins. Blood gases. Electrolytes and acid – base

balance. Regulation of electrolyte content of body fluids and maintenance of pH

reabsorption of electrolytes. Acidosis & Alkaloids and their determination in clinical

laboratory.(chalk and talk)

Unit- II

Disorder of carbohydrate metabolism: Diabetes mellitus, classification, etiology,

management, laboratory investigations- GTT. HB Alc. Diabetic complications, sugar levels

in blood, threshold for glucose, factors influencing blood glucose level. Glycogen storage

diseases, pentosuria, and galactosemsia.

Disorder of protein metabplism: Alpha – fectoprotein, Amyloidosis. Cryoglobulinaemia.

Hypo and hyper immunogammaglobulinaemia.

Unit III

Disorders of lipids: Plasma lipoproteins, cholesterol, triglycerides & phospholipids in

health and disease. Hyperlipidemia, hyperlipoproteinemia.Gauchers disease. Tay – sachs and

Niemann – Pick disease, ketone bodies. Abetalipoproteinemia. Major Cardio vascular

diseases – Atheroschrosis – risk factors, pathogenesis. Laboratory diagnosis of acute

myocardial infraction.( www.med.muni.cz/patfyz/pdf/new/met)

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Inborn error of metabolism: Phenylketonuria, alkaptonuria, albinism, tyrosinosis, mape

syrup urine disease. Leish – Nyhan syndrome, sikle cell anemia.Histidinemia. Abnormalities

in Nitrogen Metabolism Uremia., porphyria and factors affecting nitrogen balance.

Unit IV

Disoders of liver kidney: Biochemical indices of hepatobiliary disease. Bile pigments –

formation of bilirubin, urobilinogen bile acids, jaundice – prehapic, hepatic and posthepatic.

Fatty liver, normal and abnormal functions of liver. Liver function tests, diseases of the liver

– hepatitis, cholestasis, cirshosis. Gallstones. Diagnostic Enzymes – Enzymes in health and

diseases. Disoders of kidney: Assessment of renal function – creatine clearance, renal

calculi, uremia and laboratory investigation of kidney disorders, renal function tests.

Unit V

Circulation disorders: Composition cells, functions of plasma proteins and lipoproteins in

diseases. Disorders of haemoglobin – thalassemia, sickle cell anemia – Microcytic,

normocytic and macrocytic anemias. Endocrine disorders: Pituitary, thyroid, adrenals and

gonads- hypo and hyper secretion of hormones. Disorders – Graves diseases and Addition

diseases.(Blended mode of teaching)

Unit VI:

Diagnosis and interpretation: Evaluation and clinical significance of: Blood gases, Various

electrolytes (Na+, K+, HCO3, etc), Urea, Uric acid. Enzymes; Alkaline phosphatase,

Alanine aminotransferase, Aspartate aminotransferase, Lactate dehydrogenase, Creatine

kinase, Amylase, Lipase. Insulin tolerance test; growth hormone stimulation test;

Adrenocorticotropin, congenital adrenal hyperplasia or hirsutism.

Recommended Books:

a. Rodney F. Boyer - (2010). Biochemistry Laboratory: Modern Theory and Techniques,

2thedition, Pearson Prentice Hall.

b. Undurti N. Das - (2011). Molecular Basis of Health and Disease, 1st edition,Springer.

c. Nanda Maheshwari – (2008). Clinical biochemistry, 1st edition, JAYPEE.

d. MN Chatterjea, Ranashinde – (2012). Textbook of Medical Biochemistry, 8th edition,

JAYPEE.

e. By William J. Marshall, S. K. Bangert – (1995). Clinical Biochemistry: Metabolic and

Clinical Aspects, 1st edition, Churchillivingstone.

f. Michael Lieberman, Allan D. Marks – (2009). Marks' Basic Medical Biochemistry: A

Clinical Approach, 3rd edition,Lippincott Williams & Wilkins.

g. Miriam D. Rosenthal, Robert H. Glew – (2009). Medical Biochemistry: Human

Metabolism in Health and Disease, 1st edition, Wiley.

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COURSE OUTCOME

1. An advanced understanding and applied knowledge of the theory and practice of

clinical biochemistry.

2. The student will be able to describe the structure, function and metabolic pathways

for carbohydrates, amino acids and lipids.

3. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of

diabetes.

4. Explain the metabolism of lipoproteins, medical problems associated with abnormal

lipoprotein levels and therapeutic agents used to treat lipid disorders.

5. To make the students biochemistry of membranes including chemical composition

and structure of biological membranes, as well as drug transporters.

6. To impart thorough knowledge about the biochemical basis of various diseases and

disorders.

7. To study various diagnostic and therapeutic methodologies available for diseases and

disorders. Students can apply biochemistry concepts to solve clinical scenarios.

8. Describe intercellular and intracellular signal transductions and explain the molecular

mechanism of drug actions.

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BC304 - LABORATORY COURSE III

(Core 11)

SEM: III Lecture/Week: 6

BC304 Credits: 4

Objectives

i. The overall aim of this course is that the student should gain a basic working

knowledge SDS PAGE, WESTERN BLOTTING techniques.

ii. This course helps in enhancing students skill in molecular techniques which will help

them to fetch projects outside the department

iii. The student would able to describe the priciples and methods almost all the molecular

techniques.

iv. Students will be exposed to instruments used in molecular study.

v. Aims to Develop critical thinking skills/ laboratory techniques so as to be capable of

designing, carrying out, interpreting scientific experiments

1. Deriving Gene sequence from N BLAST

2. Designing primers, online software for primer design

3. Gradient PCR

4. Agarose gel

5. Isolation of plasmid DNA

6. Digestion of plasmid with restriction enzyme

7. DNA ligation

8. Transformation of plasmid construct to vector cells

9. DNA and protein over expression

10. SDS-PAGE Electrophoresis

11. Western blot

12. Assay of Alkaline phosphatase activity

13. Effect of pH and Temperature on enzyme activity

14. Determination of Vmax and Km for enzyme activity

COURSE OUTCOME:

1.The overall aim of this course is that the student should gain a basic working

knowledge SDS PAGE, WESTERN BLOTTING techniques.

2.This course helps in enhancing students skill in molecular techniques which will

help them to fetch projects outside the department

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3.The student would able to describe the priciples and methods almost all the

molecular techniques.

4.Students will be exposed to instruments used in molecular study.

5.Aims to Develop critical thinking skills/ laboratory techniques so as to be capable

of designing, carrying out, interpreting scientific experiments.

6.Students will use current biochemical and molecular techniques to plan and carry

out experiments. They will generate and test hypotheses, analyze data using statistical

methods where appropriate, and appreciate the limitations of conclusions drawn from

experimental data. Trouble-shooting will be stressed in classes and labs.

7.Students will be knowledgeable in proper procedures and regulations in handling

and disposal of chemicals. Assessment of this learning outcome occurs in every laboratory

course.

8.Students will learn to design a Primer, basics of proteiomics and genomics.

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BC3ED - DEVELOPMENTAL BIOLOGY

(Non major 2)

SEM: III Lecture/Week: 3

BC3ED Credits: 2

Objectives

i. To understand the molecular and cellular mechanisms of development and learn

about basic embryology

ii. To understanding the students will be able to generally describe the concepts of

cellular competence, induction, specification, commitment and differentiation in

embryonic development.

iii. To recognize the how to explain at least two concepts in developmental biology that

overlap with other sciences, such as stem cell research, cancer research, evolutionary

sciences, or neuroscience.

iv. Students will be able to discern and summarize the current state of knowledge on a

given topic, construct pioneering research questions on that topic, and propose

experiments aimed at answering those questions.

v. To make the students how the knowledge in genetics, evolutionary biology, cell

biology, developmental biology, physiology and ecology.

Unit- I

Emergence of evolutionary thoughts: Lamarks; Darwin – concepts of variation,

adaptation, struggle, fitness and natural selection; Mendelism; spontancity of mutations; the

evolutionary synthesis, Origin of cells and unicellular evolution; Origin of basic biological

molecules; abiotic synthesis of organic monomers and polymers; concept of Oparin and

Haldane; experiment of Miller (1953); the first cell; evolution of prokaryotes; origin of

eukaryotic cells; evolution of unicellular eukaryotes; anaerobic metabolism, photosynthesis

and aerobic metabolism.

Unit - II

Basic concepts of development: Potency, commitment, specification, induction,

competence, determination and differentiation; morphogenetic gradients; cell fate and cell

lineages; stem cells; genomic equivalence and the cytoplasmic determinants; imprinting;

mutants and transgenics in analysis of development.( cmb.i-

learn.unito.it/mod/book/tool/print/index.php)

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Unit - III

Gametogenesis, Fertilization and early development: Production of gametes, cell surface

molecules in sperm-egg recognition in animals; embryo sac development and double

fertilization in plants; zygote formation, cleavage, blastula formation,embryonic fields,

gastrulation and formation of germ layers in animals; embryogenesis, establishment of

symmetry in plants; seed formation and germination.(Blended mode)

Unit - IV

Morphogenesis and organogenesis in animals: Cell aggregation and differentiation in

Dictyostelium; axes and pattern formation in Drosophila, organogenesis – vulva formation

in Caenorhabditiselagans; eye lense induction, limb development and regeneration in

vertebrates; differentiation of neurons, post embryonic development- larval formation,

metamorphosis; environmental regulation of normal development; sex determination.

Unit V:

Morphogenesis and organogenesis in plants: Organization of shoot and root apical

meristem; shoot and root development; lead development and phyllotaxy; transition to

flowering, floral development in Arabidopsis and Antirrhunum.(Chalk and talk)

Unit VI:

Medical implications of developmental biology-genetic errors/ teratogenesis/ stem cell

therapy.

Recommended Books:

1. Principles of Development. 3rd edition, by L. Wolpert, 2006, Oxford University

press, incorporated.

2. Developmental Biology. 3rd edition, by Lewis Wolpert, 2006, Oxford University

Press, USA

3. Developmental Biology, 6th edition by Scott Gillbert, 2000, Sunderland

(MA): Sinauer Associates; ISBN-10: 0-87893-243-7

4. Evolutionary developmental biology, 2nd edition by Brain K. Hall. 1998,

Springer;ISBN-10: 0412785803

COURSE OUTCOME:

1. To Understand the molecular and cellular mechanisms of development and

learn about basic embryology

2. To understanding the students will be able to generally describe the concepts

of cellular competence, induction, specification, commitment and

differentiation in embryonic development.

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3. To understand the how to explain at least two concepts in developmental

biology that overlap with other sciences, such as stem cell research, cancer

research, evolutionary sciences, or neuroscience.

4. Students will be able to discern and summarize the current state of knowledge

on a given topic, construct pioneering research questions on that topic, and

propose experiments aimed at answering those questions.

5. To make the students how to understand the knowledge in genetics,

evolutionary biology, cell biology, developmental biology, physiology and

ecology.

6. It is useful for awareness of scientific methods and research skills used to

investigate cell & developmental biology problems

7. To awareness of ethical issues in cell and developmental biology research,

particularly in relation to stem cells, in vitro fertilisation and assisted

reproductive technologies.

8. Students can understand the capacity to evaluate and synthesise information

from a wide range of sources in order to communicate ideas, concepts and

construct arguments in both non-scientific and scientific language.

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PROJECT DISSERTATION

SEM: III Lecture/Week:

30

BC401 Credits: 20

Each candidate shall be required to take up a Project Work; submit Project Report at

the end of the second year. The Head of the Department shall assign the Guide who in

turn will suggest the Project Work to the student in the beginning of fourth semester.

Two typed copies of the Project Report shall be submitted to the Department on or

before the date fixed by the Department Head.

The Dissertation will be evaluated by Examiners, nominated by the Department. The

candidate concerned will have to defend his project in a Viva-Voce examination

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ELECTIVE PAPERS I & II

BC203 - ECOLOGY AND ENVIRONMENTAL BIOLOGY (ELECTIVE)

Objectives:

To study the physical and biological characters of the environment and the inter-

relationship between biotic and abiotic components of nature as well as relationship among

the individuals of the biotic components

Unit - I

The Environment: definition, types of environment and their importance: physical

environment; biotic environment; social environment; biotic and abiotic interactions.

Ecology: scope of ecology; historical background; ecology in India; terminology of ecology;

basic concepts of ecology.(Flipped mode)

Unit - II

Environmental Complex: Environmental and ecological factors-Direct and indirect factors;

four categories of ecological factors-climatic, topographic, edaphic and biotic factors;

interaction of ecological factors. Species Interactions: Types of interactions, interspecific

competition, herbivory, carnivory, pollination, symbiosis. Habitat and Niche: Concept of

habitat and niche; niche width and overlap; fundamental and realized niche; resource

partitioning; character displacement.(Blended mode)

Unit- III

Population Ecology: Characteristics of a population; population growth curves; population

regulation; life history strategies (r and K selection); concept of metapopulation – demes and

dispersal, interdemic extinctions, age structured populations. Community Ecology: Nature of

communities; community structure and attributes; levels of species diversity and its

measurement; edges and ecotones. Ecological Succession: Types; mechanisms; changes

involved in succession; concept of climax.

Unit - IV

Ecosystem Ecology: Ecosystem structure; ecosystem function; energy flow and mineral

cycling (C, N, and P); primary production and decomposition; structure and function of

some Indian ecosystems: terrestrial (forest, grassland) and aquatic (fresh water(, marine,

eustarine). Biogeography: Major terrestrial biomes; theory of island biogeography;

biogeographical zones of India.(https://study.com/academy/lesson/ecosystem-ecology-

definition-lesson)

Unit - V

Applied Ecology: Environmental pollution; global environmental change; biodiversity:

status, monitoring and documentation; major drivers of biodiversity change; biodiversity

management approaches. Conservation Biology: Principles of conservation, major

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approaches to management, Indian case studies on conservation/management strategy

(Project Tiger, Biosphere reserves).

Unit VI:

Waste Management: Sources, generation, classification & composition of solid wastes. Solid

waste management methods - Sanitary land filling, Recycling, Composting, Vermi-

composting, Incineration, energy recovery from organic waste. Hospital Waste

Management, Hazardous Waste Management & Handling rules, 1989 & 2000

(amendments).

Recommended Books:

1. Ecology and Environment - PD. Sharma, Rastogi Publications, 7th edition (2007).

2. Ecology-from individuals to ecosystems – Michael Begon, Colin R, Townsend and John

L Harper, Blackwell publishing - 4th edition (2006)

3. Ecology-the plants, animals and the environment-Michael Allaby, Facts on file 1st edition

(2009)

4. Ecology-Robert E Ricklefs, W.H.Freeman Publisher, Fourth edition (2000)

COURSE OUTCOME:

9. To study the physical and biological characters of the environment and the

inter-relationship between biotic and abiotic components of nature as well as

relationship among the individuals of the biotic components

10. To understanding of current environmental issues and how global problems

affect us locally.

11. Describe the ecological and evolutionary influence of abiotic factors on

organisms and how these factors affect the distribution and abundance of

species.

12. To understanding of core ecological principles, and define scientific

principles and concepts as related to environmental studies and sustainability.

13. Students should be able to demonstrate an understanding of environmental

interrelationships and of contemporary environmental issues.

14. To study the extinct species and the cause related to it.

15. Students will able to differentiate the past world environment with the present

and will think on evolution.

16. Students will learn at the end of the course to conserve the nature and will be

able to develop new strategies to preserve the sources of life.

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BC205 BIOINFORMATICS

Objective:

i. The purpose of studying this paper is to apply computational facility in different

fields of life sciences, physical and chemical sciences.

ii. After completion, students could learn drug designing through computer based

modification programs using synthetic or natural source.

iii. Most important application of Bioinformatics is in the field of drug discovery where

it reduces more than 60% of the time, money and labor.

Unit-I

Bioinformatics: An overview, Definition & History; Bioinformatics databases & tools on

the Internet- NCBI, EBI, PIR, Swiss-Prot, GenBank ; pattern and motif searches- BLOCKS,

PRINTS, PFAM.( https://www.britannica.com/science/bioinformatics)

Unit-II

Proteins Amino acids: Levels of protein structure – Ramachandran Map. Protein

Secondary structure prediction - Chou-Fasmann rules, Gamier-Osguthorpe-Robson (GOR)

methods; Predicting 3D structure – homology modeling, threading - fold recognition and ab

initio methods - Rosetta – CASP.( Blended mode)

Unit-III

Biological Sequence analysis: Pairwise sequence comparison – Sequence queries against

biological databases – BLAST and FASTA - Multiple sequence alignments –Phylogenetic

alignment.

Algorithms and Matrices: Scoring matrices- PAM and BLOSUM; dynamic programming

Algorithms, Needleman and Wunsch, Smith-Waterman;

Unit-IV

Protein structure visualization tools: RasMol, HEX, Argus Lab Swiss PDB Viewer -

Structure –Classification, alignment and analysis – SCOP, CATH, FSSP, UNIX.(Flipped

mode)

Unit-V

Functional Genomics (Metabolism and Regulation) in Biochemistry : Sequencing

genomes– Genome databases on the web, Prokaryotic Genome Database with comparison

with Human genome, HGP, GENECLUSTER, DNA Microarray, SWISS-2DPAGE

Database, TIGR,WIT, CYTOSCAPE and DRUG DISCOVERY.

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Unit VI:

Current Advancements in Bioinformatics: Introduction to System Biology, Structural

Biology, Structural bioinformatics, Chemoinformatics, Immunoinformatics.

Reference Books

1. Bioinformatics-Sequence and Genome Analysis- David W.Mount, Cold Spring Harbor

Laboratory Press (2004).

2. Introduction to Bioinformatics, Attwood, T.K. and D.J. Parry-Smith, Pearson Education

Ltd., New Delhi (2004).

3. Bioinformatics – Westhead, D.R., Paris J.H. And R.M. Twyman, Instant Notes: Viva

Books Private Ltd, New Delhi (2003).

4. Introduction to Bioinformatics, Arthur M. Lesk, Oxford University Press, New Delhi

(2003).

5. Bioinformatics- Sequence, structure and databanks, Higgins D. and W. Taylor (Eds),

Oxford University Press, New Delhi (2000).

6. Bioinformatics; A practical Guide to the Analysis of Genes and Proteins, Wiley-

Interscience, Baxevanis, A. and B.F. Ouellette , Hoboken, NJ (1998).

7. Introduction to computational Biology, Michael, S. Waterman, Chapman & Hall, (1)

COURSE OUTCOME:

1. The student can explain which type of data is available from the most

common protein sequence and structure databases (UniProt, GenBank,

Protein Data Bank, CATH).

2. The candidate can explain the theories underlying the most common

methods for sequence searches and sequence alignments, and in particular

knows the principle and main steps for pairwise and multiple sequence

alignments;

3. The student can explain and is able to apply the main steps of dynamic

programing for/to simple alignments of short sequences;

4. The student can list methods to uncover structure-function relationship in

proteins and knows their underlying principles;

5. The student can explain the principles of computational methods for the

prediction of secondary structure elements from protein sequence,

prediction and modeling of three-dimensional protein structures

(homology modeling, threading and ab initio methods).

6. select and apply the most appropriate bioinformatics sequence or structure

database to retrieve or search data given a specific question in molecular

biology;

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7. select and apply the most appropriate method for aligning sequences,

visualizing and analyzing protein structures, predicting secondary

structure elements and modeling protein structures from sequence.

8. Using their theoretical knowledge about the most commonly used

bioinformatics methods, the student is able, if encountering a new online

tool, to get a general understanding of its underlying principle.

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BC206 BIOSTATISTICS

Objectives:

The course emphasizes on various statistical methods and its significance.

The students are expected to understand the concepts and solve relevant problems

pertaining to each topic.

To provide sufficient background to be able to interpret statistical results in research.

Unit- I

Statistical survey: Organizing, planning and executing the survey. Source of data - Primary

and secondary data, collection, observation, interview, enquiry forms, questionnaire

schedule and check list. Classification and tabulation of data. Diagrammatic and graphic

presentation of data.(Blended mode of teaching)

Unit-II

Measures of central tendency : Arithmetic mean, median, mode, quartiles, deciles and

percentiles. Measures of variation - range, quartile deviation, mean deviation, standard

deviation, Coefficient of variation. Correlation analysis - Scatter diagram, Karl's Pearson's

coefficient of correlation and Spearman's rank method. Regression analysis.(Problem based

learning)

Unit-III

Probability: Definition, concepts, theorems (proof of the theorems not necessary) and

calculations of probability - Simple problems. Theoretical distributions – Binomial, Poisson

and normal distribution - Simple problems (proof of the theorems not necessary).(problem

based learning)

Unit-IV

Sampling distribution and test of significance: Concepts of sampling, Testing of

hypothesis, errors in hypothesis testing, standard error and sampling distribution, sampling

of variables (large samples and small samples.). Student's "t" distribution and its

applications. Chi-square test and goodness of fit. Analysis of variance - one way and two

way classification. Duncan's Multiple Range test. Design of experiment- Completely

randomized block design, Randomized block design.

Unit-V

Scientific Methodology: Selection of research problems – hypothesis – definition and

characteristics. Experimental approaches – biological, physical and chemical methods.

Sources of information: Journals, e-journals, books, biological abstracts, Preparation of

index cards, Review writing, Article writing – structure of article. Selection of journals for

publication- Impact factor – Citation index and H index. Proposal writing for funding.IPR

and Patenting – Concept and types.

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Unit VI:

Basic statistics: Mathematical Expectation and Generating Functions, Definition and

its properties-moments, addition and multiplication, theorem of expectation. Conditional

expectation and conditional variance. Moments generating function, cumulant generating

function, probability, generating function along with their properties.

Reference Books:

1. Statistical Methods, 4th Edition- Gupta, S.P, Sultan Chand & Son Publishers. 2012.

2. Biostatistical Analysis, 5th Edition- Zar, J.H, Pearson Education, 2010.

3. Biostatistics - Daniel, W.W. A Foundation for Analysis in Health Sciences, 10th Edition,

John Wiley and Sons, Inc., 1999.

COURSE OUTCOME:

1. Select from, use and interpret results of, descriptive statistical methods effectively;

2. Demonstrate an understanding of the central concepts of modern statistical theory

and their probabilistic foundation;

3. Select from, use, and interpret results of, the principal methods of statistical inference

and design;

4. Communicate the results of statistical analyses accurately and effectively;

5. Make appropriate use of statistical software.

6. Read and learn new statistical procedures independently

7. The students will be able to estimate and interpret three alternative measures of

association between binary exposures and binary outcomes and discuss the relative

merits of each measure for a given research question.

8. The student can explain the basis of the linear regression model, fit a linear

regression model using standard statistical software, assess the fit of the model, and

interpret the results.

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BC207- CHROMATIN AND EPIGENETICS

Objective:

This an elective course for Biochemistry majors. The objective of this course is to

provide students with a solid foundation in both the principles of epigenetics and

experimental research by emphasizing the use of primary research articles and focusing on

developing analytical scientific reading and writing skills to focus on the current questions

in epigenetics and how they are being addressed experimentally.

Unit-I

Chromatin structure: DNA and histones, nucleosome, organization of nucleosome in

chromatin, chromosomal architecture, modulation of chromosome structure, histones,

chromatin and nuclear assembly, transcription in chromatin, chromatin remodeling

machines. (www.abcam.com/epigenetics/chromatin-structure-and-function)

Unit-II

Epigenetics: Introduction to epigenetics, basic concept overview and brief history of the

field, Epigenetic modifications and gene expression: DNA methylation, DNA acetylation,

Lost in translation: Non-coding RNAs in Epigenetics.(Blended mode of teaching)

Unit-III

Linking epigenetic modifications: Chromatin remodelling and transcription, Model animal

systems for studying epigenetic regulation, Genomic imprinting in mammals, multiple layers

of epigenetic regulation; genome-wide analysis of epigenetic markers.

(https://www.whatisepigenetics.com/chromatin-remodeling)

Unit-IV

Epigenetics and the environment: Gene-environment interactions, environmental

epigenomics, interplay of genome rearrangement and environment during development,

Epigenetic programming in cell renewal and pluripotency.

Unit-V

Epigenetics in disease:

Epidemiology of health, epigenetics and endocrine diseases, Environmental

epigenetics and obesity, Epigenetics and cancer, Epigenome and aging, epigenetics and

cardiovascular disease, epigenetics and brain, Epigenetics and microRNA, Epigenetics in

drug discovery.

Unit VI:

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The Histone Code: Biochemistry of Modifying Enzymes, Binding Proteins and

RNAs in Chromatin Regulation (protein-protein, protein-nucleic acids interactions, complex

purification)

Text Book:

Chromatin and Gene Regulation: Molecular Mechanisms in Epigenetics by B. M.

Turner (2008)

Reference book:

1. Epigenetics and Chromatin edited by Philippe Jeanteur (2008)

2. Epigenetics: The Death of the Genetic Theory of Disease Transmission by Joel D.

Wallach, Ma Lan, Gerhard N. Schrauzer (2014)

3. epigenetic epidemiology edited by Karin B. Michels - 2012

4. Epigenetics in human diseases edited by Trygve Tollefsbol (2012)

COURSE OUTCOME:

1. Understand differences between Mendelian and epigenetic inheritance

2. Understand DNA methylation regulates gene expression

3. Understand how chromatin modifications and remodelling regulate gene

expression

4. Understand the role of non-coding RNAs in epigenetic regulation

5. Understand how epigenetic modifications are propagated

6. Understand the research process from hypothesis generation to final presentation

of results

7. Be able to generate testable research questions from observations.

8. Be able to design a controlled experiment to test a hypothesis and to present

findings of a primary research paper and indicate their significance/limit

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BC303 - CLINICAL BIOCHEMSITRY (ELECTIVE)

Objective

i. An advanced understanding and applied knowledge of the theory and practice of

clinical biochemistry;

ii. The student will be able to describe the structure, function and metabolic pathways

for carbohydrates, amino acids and lipids.

iii. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of

diabetes.

iv. To make the students biochemistry of membranes including chemical composition

and structure of biological membranes, as well as drug transporters

v. To impart thorough knowledge about the biochemical basis of various diseases and

disorders

Unit -I

Introduction to Biochemical laboratory: Roles of biochemical laboratory. Mechanization

and amomation in clinical biochemistry. Quality control in clinical laboratories. Total

laboratory uncertainty. Accuracy and precision. Selection and optimization of laboratory

methods, Clinical evaluvation of laboratory methods.

Biochemical analysis in urine. Clinical biochemical analysis of proteins. Plasma protein

spectrum during inflammation, paraproteins. Blood gases. Electrolytes and acid – base

balance. Regulation of electrolyte content of body fluids and maintenance of pH

reabsorption of electrolytes. Acidosis & Alkaloids and their determination in clinical

laboratory. .(chalk and talk)

Unit -II

Disorder of carbohydrate metabolism: Diabetes mellitus, classification, etiology,

management, laboratory investigations- GTT. HB Alc. Diabetic complications, sugar levels

in blood, threshold for glucose, factors influencing blood glucose level. Glycogen storage

diseases, pentosuria, and galactosemsia.

Disorder of protein metabplism: Alpha – fectoprotein, Amyloidosis. Cryoglobulinaemia.

Hypo and hyper immunogammaglobulinaemia.

Unit - III

Disorders of lipids: Plasma lipoproteins, cholesterol, triglycerides & phospholipids in

health and disease. Hyperlipidemia, hyperlipoproteinemia.Gauchers disease. Tay – sachs and

Niemann – Pick disease, ketone bodies. Abetalipoproteinemia. Major Cardio vascular

diseases – Atheroschrosis – risk factors, pathogenesis. Laboratory diagnosis of acute

myocardial infraction.

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Inborn error of metabolism: Phenylketonuria, alkaptonuria, albinism, tyrosinosis, mape

syrup urine disease. Leish – Nyhan syndrome, sikle cell anemia.Histidinemia. Abnormalities

in Nitrogen Metabolism Uremia., porphyria and factors affecting nitrogen balance. .(

www.med.muni.cz/patfyz/pdf/new/met)

Unit - IV

Disoders of liver kidney: Biochemical indices of hepatobiliary disease. Bile pigments –

formation of bilirubin, urobilinogen bile acids, jaundice – prehapic, hepatic and posthepatic.

Fatty liver, normal and abnormal functions of liver. Liver function tests, diseases of the liver

– hepatitis, cholestasis, cirshosis. Gallstones. Diagnostic Enzymes – Enzymes in health and

diseases. Disoders of kidney: Assessment of renal function – creatine clearance, renal

calculi, uremia and laboratory investigation of kidney disorders, renal function tests.

Unit - V

Circulation disorders: Composition cells, functions of plasma proteins and lipoproteins in

diseases. Disorders of haemoglobin – thalassemia, sickle cell anemia – Microcytic,

normocytic and macrocytic anemias. Endocrine disorders: Pituitary, thyroid, adrenals and

gonads- hypo and hyper secretion of hormones. Disorders – Graves diseases and Addition

diseases. (Blended mode)

Unit VI:

Diagnosis and interpretation: Evaluation and clinical significance of: Blood gases, Various

electrolytes (Na+, K+, HCO3, etc), Urea, Uric acid. Enzymes; Alkaline phosphatase,

Alanine aminotransferase, Aspartate aminotransferase, Lactate dehydrogenase, Creatine

kinase, Amylase, Lipase. Insulin tolerance test; growth hormone stimulation test;

Adrenocorticotropin, congenital adrenal hyperplasia or hirsutism.

Recommended Books:

I. Rodney F. Boyer - (2010). Biochemistry Laboratory: Modern Theory and Techniques,

2thedition, Pearson Prentice Hall.

II. Undurti N. Das - (2011). Molecular Basis of Health and Disease, 1st edition,Springer.

III. Nanda Maheshwari – (2008). Clinical biochemistry, 1st edition, JAYPEE.

IV. MN Chatterjea, Ranashinde – (2012). Textbook of Medical Biochemistry, 8th edition,

JAYPEE.

V. By William J. Marshall, S. K. Bangert – (1995). Clinical Biochemistry: Metabolic and

Clinical Aspects, 1st edition, Churchillivingstone.

VI. Michael Lieberman, Allan D. Marks – (2009). Marks' Basic Medical Biochemistry: A

Clinical Approach, 3rd edition,Lippincott Williams & Wilkins.

VII. Miriam D. Rosenthal, Robert H. Glew – (2009). Medical Biochemistry: Human

Metabolism in Health and Disease, 1st edition, Wiley.

COURSE OUTCOME:

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1. An advanced understanding and applied knowledge of the theory and practice of

clinical biochemistry.

2. The student will be able to describe the structure, function and metabolic pathways

for carbohydrates, amino acids and lipids.

3. To learn the alterations in lipid and carbohydrate metabolism that occur as a result of

diabetes.

4. Explain the metabolism of lipoproteins, medical problems associated with abnormal

lipoprotein levels and therapeutic agents used to treat lipid disorders.

5. To make the students biochemistry of membranes including chemical composition

and structure of biological membranes, as well as drug transporters.

6. To impart thorough knowledge about the biochemical basis of various diseases and

disorders.

7. To study various diagnostic and therapeutic methodologies available for diseases and

disorders. Students can apply biochemistry concepts to solve clinical scenarios.

8. Describe intercellular and intracellular signal transductions and explain the molecular

mechanism of drug actions.

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BC305 MEMBRANE BIOCHEMISTRY

Objectives:

➢ To understand the biological importance membrane biochemistry.

➢ To study the importance of membrane transport.

Unit-I

Biological membrane: Structure, and assembly: constituents, bacterial cell envelope,

asymmetry flip flop, protein lipid interaction, factors affecting physical properties of

membranes. Membrane models: biological and physical models: energetics and

transduction phenomena, biochemical chemiosmotic hypothesis of Mitchell.(Chalk and

talk)

Unit-II

Physical organization of Membrane Bilayers: Human erythrocyte membrane as a

prototype plasma membrane, role of cytoskeleton in organization of bilayers. Liposomes;

preparation, properties and application in membrane biochemistry. Asymmetry of lipid

distribution in bacterial, plant, and animal membranes, Lateral heterogeneity of membrane

lipids; lipid domains, lipid rafts, Non bilayer lipids and their role in membranes.(Blended

mode of te\ching)

Unit-III

Membrane transport: Diffusion, passive, active and facilitated, transport role of proteins in

the process, exocytosis, receptor mediated endocytosis, osmoregulation. Assembly of virus

membrane receptor.(Flipped mode)

Unit-IV

Specialized mechanism for transport of macromolecules: Na, H dependent processes

and phosphotranferase synthesis, gap junctions, nuclear pores, toxins, control of

transport processes, binding proteins, hormone effects and the role of lipids. Role of Na, K

ATPase and the passive permeability of the plasma membrane to Na, K and Cl,

voltage and ligand gated ion channels, ATP-ADP exchanger.

Unit-V

Mechanistic action of Membrane: Molecular mechanisms, ion translocating antibiotics,

valinomycin, gramicidin, ouabain, group translocation, ionophores, electrical gradient,

energy coupling mechanism. Penetrating the defenses: how antimicrobial agents reach

their targets, cellular permeability barrier to drug penetration, some examples of

modes of penetration of antimicrobial agents, the exploitation of transport systems

in the design of new antimicrobial agents.

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UNIT VI:

Membrane asymmetry and its significance in membrane structure and function. Various

techniques to determine asymmetry. Its implications in health and disease. Its role in

membrane signalling.

Reference Books:

1. Membranes and their cellular functions- IB Filnean, R.Coleman and RH Michell, 1984,

Blackwell scientific publishers, Oxford, 3rd ed.

2. Molecular Cell Biology; Lodish et al., 7th Edn. W.H. Freeman and Co. 2012.

3. Introduction to Biological Membranes; William Still well, Elsevier 2013.

4. Biochemistry-G Zubay , Addison Wesley, 1983

5. Biochemistry, L Stryer, 3rd/4th/5th ed, 1989 , Freeman and Co. NY

6. Principles of Biochemistry –Lehninger .

7. Harper’s Illustrated Biochemistry; 27th Edn. Robert K. Murray, Daryl K. Granner, Victor

W.Rodwell , The McGraw6Hill 2006.

COURSE OUTCOME:

1. To understand the signals in proteins and mRNAs that determine their localisation to

different parts of a cell.

2. Students can be observed the mechanisms that target proteins to particular organelles

or ensure they are secreted from the cell .

3. The various types of post-translational covalent modifications of intra-cellular

proteins and how these modifications regulate protein function and stability, with

particular regard to glycosylation, acylation, prenylation and ubiquitination.

4. To understand how calcium signalling can be divided into elemental and global

events and give examples of the processes which are influenced by these events.

5. Students develop presentational skills associated with giving a short oral presentation

on a specific topic.

6. Describe the major mechanisms of cell/cell signaling in humans, including the

hierarchical nature of the neuroendocrine system.

7. Describe the mechanism of action of the major functional groups of signalling

molecules, including polypeptides (growth hormones, insulin, glucagon), steroids,

thyroxine, retinoic acid, amino acid derived signalling molecules, classical

neurotransmitters & eicosanoids.

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8. Discuss the molecular events which occur within the cell in response to the major

groups of signalling molecules and the overall physiological outcomes.

BC307 CONCEPTS IN NEUROCHEMISTRY

Objectives:

To introduce basic concepts about the organization, structure, and function of the

human central nervous system; To enable students to apply these fundamental principles

toward understanding nervous system function and dysfunction and toward clinical problem-

solving in relation to disorders that affect the nervous system, with emphasis on the central

nervous system.

PRE-REQUISITE:

Neuroscience is a stand-alone course but it is expected that students have a basic

understanding of human anatomy and physiology and the basic vocabulary of the anatomical

sciences.

Unit-I

CNS Overview: Introduction to the Brain; Overview of brain systems and general principles

of their functional organization: From cortical maps and subcortical loops to the micro-

structure of brain circuits and their interconnections. CNS Organization; CNS Topography;

Neuroembryology. VASCULATURE: Metabolism, Cerebral blood flow, CSF; Blood

Supply; Stroke.( https://www.msdmanuals.com › ... › Biology of the Nervous System)

Unit-II

CELL BIOLOGY OF NEURONS AND GLIA: Nucleus and gene expression and

regulation, Protein synthesis & translational control (including RNAi), Protein sorting &

trafficking (signal peptides, Golgi, secretory and endocytic pathways), Cytoskeleton &

transport (cytoskeleton, actin, microtubules, intermediate filaments, dendritic and axonal

localization/transport, motors and adaptor), Signaling Pathways. Mitochondria, energy

homeostasis and free radicals/energy metabolism in the neuron, Overview of glial cell

biology & myelination (types of glia, morphology and function, myelination in CNS and

PNS).(Blended mode of teaching)

Unit-III

ELECTRICAL PROPERTIES OF NEURONS: Overview of membrane structure &

membrane transport, membrane potential, Ion channels and Ion Channel activity

(electrochemical gradient), Action potentials, Propagation of action potentials along axons,

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Modulating action potential, Electrophysiological techniques for studying action potentials

and ion channels.

Unit-IV

SYNAPTIC TRANSMISSION: Overview of synaptic communication/structure of the

synapse, Neural Signaling:- Neruotransmitters; Action potentials:- Resting potential;

Excitatory; Inhibitory; Threshold; Depolarization; Hyperpolarization; Synapse: Formation;

Synaptic communication; Neural circuits, synaptic plasticity: LTP/LTD, Spike Time

dependent plasticity. Mechanism of neurotransmitter release, postsynaptic response:

electronic properties of dendrites, basic integration, Ionotropic (v) metabotrobic receptors,

Neurochemical transmission: Glutamate, GABA, Glycine, Acetylcholine (Synthesis,

storage, release and inactivation), Dopamine, Norepinephrine, epinephrine, serotonin,

histamine, Neuropeptides & atypical neurotransmitters, Electrical synapses (gap junctions).

Unit-V

DEVELOPMENT & PLASTICITY: Overview of nervous system development/

comparative embryology, Neural induction, Regionalization, Neurogenesis & migration,

Mechanisms of axon guidance & target cell recognition, Synapse formation & elimination,

Neuronal Death.(Chalk and talk)

Unit-VI

TRUAMA AND DISEASE: Development disorders; Degenerative disorders; Psychiatric

disorders; Injury disorders; Others like Epilepsy; Visual Pathways; Occular Movements;

Vascular syndromes; Sensory and Motor Syndromes.

TEXTBOOK

1. J. W. Baynes, M. H. Dominiczak, Medical Biochemistry, 2nd ed., Elsevier Mosby,

Philadelphia, New York, Toronto, 2005.

2. G. Siegel, R.W. Albess, S. Brady, D. Price, Basic Neurochemistry, 7th Edition,

Amsterdam. Tokio, 2006.

3. George J Siegel, MD, Editor-in-Chief, Bernard W Agranoff, MD, R Wayne Albers,

PhD, Stephen K Fisher, PhD, and Michael D Uhler, PhD. Basic Neurochemistry, 6th

edition Philadelphia: Lippincott-Raven; 1999.

4. Dale purves , George j. Augustine, David fitzpatrick , William c. Hall, Anthony-

samuel lamantia , James o. Mcnamara , S. Mark williams. Neuroscienc ethird edition

Publishers Sunderland, Massachusetts U.S.A, 2004.

5. Siegel, George and R. Wayne Albers, Scott Brady and Donald Price Basic

Neurochemistry, 7th edition: Molecular, Cellular and Medical Aspects Academic

Press/2005.

6. Haines, Duane Neuroanatomy - An Atlas of Structures, Sections and Systems, 5th

edition Lippincott Williams and Wilkins/2000.

REFERENCE BOOKS

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1. Afifi and Bergman, Functional Neuroanatomy, Text and Atlas, McGrawHill, 2nd

Edition, 2005.

2. Haines, Neuroanatomy: An Atlas of Structures, Sections and Systems, 7th ed. Ed.

Lippincott William and Wilkins, 2007.

3. Blumenfeld, Neuroanatomy Through Clinical Cases (Paperback), Sinauer

Associates; 2nd edition (2010).

COURSE OUTCOME:

1. Neurochemistry is the scientific study of the chemical interactions of the

brain and nervous system.

2. Ultimate goal is to understand higher brain function at a variety of levels.

3. Understand the properties of cells that make up the nervous system including

the propagation of electrical signals used for cellular communication.

4. Relate the properties of individual cells to their function in organized neural

circuits and systems.

5. Understand how the interaction of cells and neural circuits leads to higher

level activities such as cognition and behaviour.

6. An understanding of the influence of family, community, and society in the

care of people with neurological disorder.

i. Evaluate and discuss primary research literature and evaluate the validity of

hypotheses generated by others.

7. This course is providing you with the requisite skills to effectively

communicate scientific and medical information to diverse audiences.

8. Understanding pathophysiology, work-up, and treatments for Disease

Specific Knowledge.

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ED Papers

BC3ED - DEVELOPMENTAL BIOLOGY (ED PAPER)

Objectives

i. To understand the molecular and cellular mechanisms of development and learn

about basic embryology

ii. To understanding the students will be able to generally describe the concepts of

cellular competence, induction, specification, commitment and differentiation in

embryonic development.

iii. To recognize the how to explain at least two concepts in developmental biology that

overlap with other sciences, such as stem cell research, cancer research, evolutionary

sciences, or neuroscience.

iv. Students will be able to discern and summarize the current state of knowledge on a

given topic, construct pioneering research questions on that topic, and propose

experiments aimed at answering those questions.

v. To make the students how the knowledge in genetics, evolutionary biology, cell

biology, developmental biology, physiology and ecology.

Unit - I

Emergence of evolutionary thoughts: Lamarks; Darwin – concepts of variation, adaptation,

struggle, fitness and natural selection; Mendelism; spontancity of mutations; the

evolutionary synthesis, Origin of cells and unicellular evolution; Origin of basic biological

molecules; abiotic synthesis of organic monomers and polymers; concept of Oparin and

Haldane; experiment of Miller (1953); the first cell; evolution of prokaryotes; origin of

eukaryotic cells; evolution of unicellular eukaryotes; anaerobic metabolism, photosynthesis

and aerobic metabolism.(Blended mode of teaching)

Unit - II

Basic concepts of development: Potency, commitment, specification, induction, competence,

determination and differentiation; morphogenetic gradients; cell fate and cell lineages; stem

cells; genomic equivalence and the cytoplasmic determinants; imprinting; mutants and

transgenics in analysis of development.(cmlearn.unito.it/mod/book/tool)

Unit -III

Gametogenesis, Fertilization and early development: Production of gametes, cell surface

molecules in sperm-egg recognition in animals; embryo sac development and double

fertilization in plants; zygote formation, cleavage, blastula formation,embryonic fields,

gastrulation and formation of germ layers in animals; embryogenesis, establishment of

symmetry in plants; seed formation and germination.

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Unit - IV

Morphogenesis and organogenesis in animals: Cell aggregation and differentiation in

Dictyostelium; axes and pattern formation in Drosophila, organogenesis – vulva formation

in Caenorhabditiselagans; eye lense induction, limb development and regeneration in

vertebrates; differentiation of neurons, post embryonic development- larval formation,

metamorphosis; environmental regulation of normal development; sex determination.

Unit - V

Morphogenesis and organogenesis in plants: Organization of shoot and root apical meristem;

shoot and root development; lead development and phyllotaxy; transition to flowering, floral

development in Arabidopsis and Antirrhunu.(https://academic.oup.com/botlinnean/article-

pdf/.).

Unit VI:

Medical implications of developmental biology-genetic errors/ teratogenesis/ stem cell

therapy.

Recommended Books:

5. Principles of Development. 3rd edition, by L. Wolpert, 2006, Oxford University

press, incorporated.

6. Developmental Biology. 3rd edition, by Lewis Wolpert, 2006, Oxford University

Press, USA

7. Developmental Biology, 6th edition by Scott Gillbert, 2000, Sunderland

(MA): Sinauer Associates; ISBN-10: 0-87893-243-7

8. Evolutionary developmental biology, 2nd edition by Brain K. Hall. 1998,

Springer;ISBN-10: 0412785803

COURSE OUTCOME:

9. To Understand the molecular and cellular mechanisms of development and

learn about basic embryology

10. To understanding the students will be able to generally describe the concepts

of cellular competence, induction, specification, commitment and

differentiation in embryonic development.

11. To understand the how to explain at least two concepts in developmental

biology that overlap with other sciences, such as stem cell research, cancer

research, evolutionary sciences, or neuroscience.

12. Students will be able to discern and summarize the current state of knowledge

on a given topic, construct pioneering research questions on that topic, and

propose experiments aimed at answering those questions.

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13. To make the students how to understand the knowledge in genetics,

evolutionary biology, cell biology, developmental biology, physiology and

ecology.

14. It is useful for awareness of scientific methods and research skills used to

investigate cell & developmental biology problems

15. To awareness of ethical issues in cell and developmental biology research,

particularly in relation to stem cells, in vitro fertilisation and assisted

reproductive technologies.

16. Students can understand the capacity to evaluate and synthesise information

from a wide range of sources in order to communicate ideas, concepts and

construct arguments in both non-scientific and scientific language.

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BC2ED - GENETICS (ED PAPER)

Objectives

i. Identify and describe the process and purposes of the cell cycle, meiosis, and mitosis,

as well as predict the outcomes of these processes.

ii. Transmission genetics problems, make accurate predictions about inheritance of

genetic traits, and map the locations of genes

iii. To identify the parts, structure, and dimensions of DNA molecules, RNA molecules,

and chromosomes, and be able to categorize DNA as well as describe how DNA

is stored

iv. To describe what causes and consequences of DNA sequence changes and how cells

prevent these changes, as well as make predictions about the causes and effects

of changes in DNA

v. To describe applications and techniques of modern genetic technology, as well as

select the correct techniques to solve practical genetic problems

Unit - I

Introduction to Genetics: Brief history/basic concepts of genetics, Cell division and

chromosomes. Mendelian genetics/monohybrid, dihybrid cross. Mendelian

genetics/trihybrid cross, probability. Modification of Mendelian ratios/incomplete and

codominance.Modification of Mendelian ratios/incomplete and codominance.Structure of

Gene - Interaction of Gene - Commentary Factors, Supplementary Factors, Inhibitory and

Lethal Factors - Atavism. . (https://www.slideshare.net/vanessaceline/intorduction-to-

genetics)

Unit - II

Diploid chromosomes number.Sex differentiation and sex determination.The X

chromosomes, Barr bodies, the Lyon hypothesis. Aneuploidy and polyploidy: Gene deletion,

duplication, inversions and translocation. Sex Linkage in Drosopohila and Man, Sex

Influenced and Sex Limited Genes - Non-Disjunction and Gynandromorphs - Cytoplasmic

Inheritance - Maternal Effect OnLimnaea (Shell Coiling), Male Sterility (Rode's

Experiment).CO2 sensitivity In Drosophila, Kappa particles in Paramecium, Milk Factor in

Mice.(Blended mode )

Unit - III

Blood Groups and their Inheritance in Human - Linkage and Crossing Over:- Drosophila -

Morgans' Experiments - Complete and Incomplete Linkage, Linkage Groups, Crossing Over

types, Mechanisms - Cytological Evidence for Crossing Over, Mapping of Chromosomes -

Interference and Coincidence.

Unit -IV

Nature and Function of Genetic Material - Fine Structure of the Gene - Cistron, Recon,

Muton - Mutation - Molecular Basis of Mutation, Types of Mutation, Mutagens, Mutable

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and Mutator Genes. Chromosomal Aberrations - Numerical and Structural Examples from

Human.

Unit -V

Applied Genetics - Animal Breeding - Heterosis, Inbreeding, Out Breeding, Out Crossing,

Hybrid Vigour. Population Genetics, Evolutionary genetics, Hardy Weinberg Law - Gene

Frequency, Factors Affecting Gene Frequency, Eugenics, Euphenics and Euthenics,

Bioethics. www.goldiesroom.org/...)

Unit VI:

Genetic Principles and their application in medical practice; Case studies (Interacting with

patients, learning family history and drawing pedigree chart); Syndromes and disorders:

definition and their genetic basis - Cystic fibrosis and Tay Sach’s Syndrome;

Phenylketonuria and Galactosemia; Ethical issues with clinical genetics.

Recommended Books:

1. Genetics by Verma, P.S. and V. K.Aggarwal.

2. Genetics by Russell P.J.

3. Genetics analysis and principles by Brooker R.J and McGraw Hill.

4. Basic Genetics my Miglani G.S.

5. Genetics: Analysis of genes and genomes by Hartl D.L and Jones E.W.

COURSE OUTCOME:

1.Identify and describe the process and purposes of the cell cycle, meiosis, and

mitosis, as well as predict the outcomes of these processes.

2.Transmission genetics problems, make accurate predictions about inheritance of

genetic traits, and map the locations of genes.

3.To identify the parts, structure, and dimensions of DNA molecules, RNA

molecules, and chromosomes, and be able to categorize DNA as well as describe how DNA

is stored.

4.To describe what causes and consequences of DNA sequence changes and how

cells prevent these changes, as well as make predictions about the causes and effects of

changes in DNA.

5.To describe applications and techniques of modern genetic technology, as well as

select the correct techniques to solve practical genetic problems.

6.To carry out genetics laboratory and field research techniques.

7.To describe experimental results in written format both informally and in formal

manuscript format.

8.To accurately diagram and describe the processes of replication, transcription,

translation, as well as predict the outcomes of these processes"

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BC3ED-1 COMPUTATIONAL BIOLOGY

Objective:

The main objective of this course is to provide foundation in fundamental concepts,

tools and resources in Computational Biology. A sound foundation in Mathematics

algorithms and Statistics is essential for analysis of biological data. It is necessary to develop

programming skills in languages like C++, PERL, Python and Java.

Unit-I Biochemistry and Biophysics: Laws of chemistry and physics, quantum mechanics,

Structure of atom, molecular orbitals and covalent bonds, molecular interactions,

Steriochemistry, Structure of Protein, DNA and RNA (primary/secondary/tertiary structure;

atoms, bonds, backbones, torsion angles), Amino and Nucleic Acids (hydrophobicity,

polarity, charge, aromatic rings), Force Fields (charge, radii, electrostatics, van der Waals,

stacking, hydrogen bonds), Structure Determination (Crystallography, NMR), Structure

Modeling (Folding, docking, dynamics, mutagenesis effects).(Blended of teaching)

Unit-II Applied mathematics: Numerical descriptive techniques: Measures of central

tendency, Correlation and Regression, Matrices and Linear Algebra, Vector Analysis,

Trigonometry and Analytical Geometry, Calculus, Numerical Methods.(Problem based

learning)

Unit-III Algorithms: Algorithms in Computing, Algorithm design techniques, Greedy

Algorithms, Dynamic Programming Algorithms, Divide-and-Conquer Algorithms,

Combinatorial Pattern Matching, Expectation and Maximation, Genetic Algorithm Hidden

Markov Models, Clustering and Trees.

Unit-IV Computing: Programming languages, Algorithm, Flowchart, Compiling, Testing

and Debugging, Documentation – Data structures – Array, Stack, Queue, Linked List

concepts, Programming in C and C++, Perl & Bioperl, Java Basics.

Unit-V Modeling tools and resources: Protein Databases: BLAST/NCBI, Protein Data

Bank, SCOP, OrthoMCL, • Structure: PyMol, ConSurf, Modeller, TMalign, DALI, DSSP,

Macromolecular Docking/Interfaces: ZDOCK, PatchDock, KFC2, Molecular Dynamics:

OpenMM (CHARMM, AMBER, GROMACS FFs), Electrostatics: PDB2PQR, APBS.

Unit VI:

Information search and data retrieval Introduction, tools for web search, data

retrieval tools, data mining of biological databases, biological databases, difference between

primary, secondary and tertiary databases, types of databases. Probabilistic information

retrieval, language models for information retrieval, managing bioinformatics tools,

command line sequence extraction and analysis.(Student led learning)

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Text Book:

1. Biostatistics (9th Ed.) by Wayne W. Daniel. John Wiley. 2004

2. Programming in ANSI C (4th Ed.) by E. Balagurusamy. Tata McGrawHill

Publishing Company Limited. 2007

3. Algebra (3rd Ed.) by Serge A. Lang. Pearson education. 2003

4. Introduction to Calculus & Analysis, Vol I and II by Richard Courant & Fritz John,

Springer publisher.1999.

5. An introduction to bioinformatics algorithms by Neil C. Jones, Pavel Pevzner. MIT

Press. 2004

Reference book:

1. Statistical Methods by N. G. Das, Vol: I and II. The McGraw-Hill Companies. 2009

2. Beginning PERL for Bioinformatics by James Tisdall. O’Reilly publications.2001

3. Basic mathematics by Serge A. Lang, Springer publisher. 1988.

COURSE OUTCOME:

1. Explain the origin, rationale and uses of large datasets used to study biological

processes in living organisms.

2. Perform computational analyses of biological datasets and relate the results to core

principles in biology.

3. Use computational methods to help execute a biological research plan.

4. Analyse biological problems from global and ethical impact perspectives (impact of

computational biology methods).

5. Students will also appreciate diverse applications in machine learning, robotics,

communications, biology, ecology, brain science, sociology, and economics.

6. The course will emphasize the fundamental underpinnings of network science to

graph-theoretic concepts and graph algorithms and so will focus on algorithmic,

computational, and statistical methods of network science.

7. The course will go beyond the strictly structural concepts of small-world and scale-

free networks, focusing on dynamic network processes such as epidemics,

synchronization, or adaptive network formation.

8. The program provides the student with a broad scientific foundation

suitable immediately upon graduation for careers in biological information analysis

in fields like: bioinformatics, the biotechnology industry, medicine, research in

computational biology or bioinformatics, healthcare, or the chemical and molecular

disciplines.