1 20.6 protein structure: tertiary and quaternary structure 20.7 protein hydrolysis and denaturation...

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1 20.6 Protein Structure: Tertiary and Quaternary Structure 20.7 Protein Hydrolysis and Denaturation Chapter 20 Amino Acids and Proteins

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Page 1: 1 20.6 Protein Structure: Tertiary and Quaternary Structure 20.7 Protein Hydrolysis and Denaturation Chapter 20 Amino Acids and Proteins

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20.6 Protein Structure: Tertiary and Quaternary Structure

20.7 Protein Hydrolysis and Denaturation

Chapter 20 Amino Acids and Proteins

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The tertiary structure: Gives a specific overall shape to a protein. Involves interactions and cross links between

different parts of the peptide chain. Is stabilized by

Hydrophobic and hydrophilic interactions Salt bridges

Hydrogen bondsDisulfide bonds

Tertiary Structure

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Tertiary Structure

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Tertiary Structure

The interactions of the R groups give a protein its specific three-dimensional tertiary structure.

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Globular Proteins

Globular proteins: Have compact,

spherical shapes. Carry out synthesis,

transport, and metabolism in the cells.

Such as myoglobin store and transport oxygen in muscle.

Myoglobin

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Fibrous Proteins

Fibrous proteins: Consist of long, fiber-like shapes. Such as alpha keratins make up hair, wool,

skin, and nails. Such as feathers contain beta keratins with

large amounts of beta-pleated sheet structures.

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Quaternary Structure The quaternary structure

contains two or more tertiary subunits.

Hemoglobin contains two alpha chains and two beta chains.

The heme group in each subunit picks up oxygen for transport in the blood to the tissues.

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Summary of Structural Levels

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Protein hydrolysis: Splits the peptide bonds to give smaller

peptides and amino acids. Occurs in the digestion of proteins. Occurs in cells when amino acids are needed

to synthesize new proteins and repair tissues.

Protein Hydrolysis

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Hydrolysis of a Dipeptide

In the lab, the hydrolysis of a peptide requires acid or base, water and heat.

In the body, enzymes catalyze the hydrolysis of proteins.

+

H3N CH COH

OCH3

+

H2O, H+

++

heat,

CH2

OH

H3N CH C

O

N

H

CH C

O

OH

CH3

CH2

OH

CH C

O

OHH3N

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Denaturation involves the disruption of bonds in the secondary, tertiary and quaternary protein structures.

Heat and organic compounds break apart H bonds and disrupt hydrophobic interactions.

Acids and bases break H bonds between polar R groups and disrupt ionic bonds.

Heavy metal ions react with S-S bonds to form solids.

Agitation such as whipping stretches chains until bonds break.

Denaturation

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Denaturation of protein occurs when:

An egg is cooked. The skin is wiped with

alcohol. Heat is used to cauterize

blood vessels. Instruments are sterilized in

autoclaves.

Applications of Denaturation