organic chemistry ap biology. carbohydrates how do you recognize a carb? function?
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Organic ChemistryOrganic Chemistry
AP BiologyAP Biology
CarbohydratesCarbohydrates
How do you recognize a carb?How do you recognize a carb?
Function?Function?
Structure/Function RelationshipsStructure/Function RelationshipsWhy are carbs good for Energy?Why are carbs good for Energy?
Why short term?Why short term?
Specific structure/function relationshipsSpecific structure/function relationships
Glycogen
LipidsLipids
Structure?Structure?
Functions?Functions?
Examples?Examples?
Structure/Function RelationshipsStructure/Function RelationshipsFats – saturated and unsaturatedFats – saturated and unsaturatedCholesterolCholesterolSteroid HormonesSteroid HormonesWaxWaxMucusMucus
ProteinsProteins
Structure?Structure?
Globular vs. Fibrous Proteins?Globular vs. Fibrous Proteins?
Functions of Structural Proteins?Functions of Structural Proteins?
Functions of Globular Proteins?Functions of Globular Proteins?
Structure/Function Relationships?Structure/Function Relationships?
Fibrous vs. Globular ProteinsFibrous vs. Globular Proteins
Protein FoldingProtein FoldingPrimary StructurePrimary Structure – straight chain of aa – not – straight chain of aa – not functionalfunctional
Secondary StructureSecondary Structure – starts to fold – alpha- – starts to fold – alpha-helix and beta pleated sheats – uncharged parts helix and beta pleated sheats – uncharged parts probably start of collapse together and the O of probably start of collapse together and the O of the acid groups form H bonds the acid groups form H bonds
with the H from the amino with the H from the amino
groupgroup
Protein Folding continuedProtein Folding continuedTertiary StructureTertiary Structure – caused by interactions of R – caused by interactions of R groups that have now been brought closer groups that have now been brought closer together by secondary folding – Functional!together by secondary folding – Functional!Held together by:Held together by:
Hydrogen bondsHydrogen bonds Disulfide bonds between cystein aaDisulfide bonds between cystein aa Hydrophobic interactionsHydrophobic interactions Ionic bondsIonic bonds
Quarternary StructureQuarternary Structure – when more than one – when more than one polypetide binds together to make the final polypetide binds together to make the final shape of the protein (ex. Hemoglobin) – shape of the protein (ex. Hemoglobin) – Functional!Functional!
DNADNA
Structure?Structure? base pairing (purine/pyrimidine, A-T, G-C, base pairing (purine/pyrimidine, A-T, G-C,
covalent bonding of backbone, H bonding covalent bonding of backbone, H bonding between basesbetween bases
Function?Function?
Structure/function relationships?Structure/function relationships?
Structure/FunctionStructure/FunctionWhy covalent bonds in backbone?Why covalent bonds in backbone? In order to code for proteins – order of the bases is In order to code for proteins – order of the bases is
most imp. The order is maintained by the backbone most imp. The order is maintained by the backbone which cannot fall apart or DNA is uselesswhich cannot fall apart or DNA is useless
Why H bonds between base pairs?Why H bonds between base pairs? Enough to hold the 2 strands together but easy Enough to hold the 2 strands together but easy
enough to sep. for replication and transcriptionenough to sep. for replication and transcription
Why purine-pyrimidine pairs Why purine-pyrimidine pairs Purines double ringed, pyr single ringed by pairing, all Purines double ringed, pyr single ringed by pairing, all along the DNA is the same width so the covalent bonds along the DNA is the same width so the covalent bonds of the backbone aren’t strainedof the backbone aren’t strained
Why do we need base pairing?Why do we need base pairing? Ensures exact copyingEnsures exact copying