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Uses
growth, repair,support, movement, transport, immunity, and coordination
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Examples
collagen, keratin, hemoglobin, antibodies, enzymes, hormones
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Amino Acids
- monomers
- 20 total
- amine + carboxyl+ hydrogen + R(rest)
- ONLY thing that changes from one amino acid to the next is R
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Linking Amino Acids
- condensation- links amino acids together
- peptide bond
- aa+aa= dipeptide
- aa x 36= polypeptide
- order determines shape, shape determines protein(function)
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20 Amino Acids
- 8- essential to diet (body can't make)
- 12- non essential to diet (body can make)
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Transamanation
body can rearrange to make certain amino acids
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Structure
- random genetic mutations
- environmental conditions (pollutants)
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Fibrous/Globular Proteins
- Fibrous- insoluble, long coiled (keratin,collagen,elastin)
- Globular- soluble, rounded structure, compact (hormones, antibodies,enzymes)
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Enzymes
- proteins that act as biological catalysts; control rate of reaction
- weaken bonds/ lower the amount of activation energy
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Globular
- active site: where they connect
- enzyme + substrate( whatever you are trying to build up/break down)
- arrangement determines what it can connect with
- "-ase"
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Lock and Key Model
every enzyme has a matching substrate
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Induced Fit Model
if enzyme and substrate are close enough, it will work
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Catabolic Reaction
1 sub → 2 products
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Anabolic Reaction
2 sub → 1 product
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Denaturating Proteins
cannot work due to change in temperature; pH can unfold a protein
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Remember
enzymes are very specific
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Primary Structures
straight
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Secondary Structures
helix (coil) or pleated sheet (fold)
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Tertiary Structures
- Polypeptide= pleated + helix working together
- > 2/3 of either pleated or helix
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Quaternary Structures
globular
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