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PROTEINS (Polymers of Amino Acids)
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20 Amino Acids Grouped by properties of their side chains Polypeptide
Non-polar (hydrophobic) Polar (hydrophilic) Acidic (-COOH grp) Basic (-NH2) Polypeptide Many amino acids linked together
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Types of Proteins Structural – ligaments, hair, horns, webs
Storage (energy) – seeds, egg whites Transportation – blood & Facillitated Diffusion Regulation – hormones: insulin & testosterone Movement/Reaction – reflex, contraction Immunology – antigens & antibodies Enzymes – speed up rxns (digestion)
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DENATURATION Protein loses its shape & no longer function Causes:
More shape changes, greater impact on its ability to function Causes: Temperature pH (toxic chemicals) Radiation Example: Sickle Cell Anemia
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MOLECULAR STRUCTURE PRIMARY Sequence of amino acids
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MOLECULAR STRUCTURE Single (point) mutations can cause problems
Normal hemoglobin: VAL – HIS – LEU – THR – PRO – GLU – GLU Sickle Cell Hemo.: VAL – HIS – LEU – THR – PRO – VAL – GLU
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MOLECULAR STRUCTURE SECONDARY A.A. chain coil or fold due H-bonds
Alpha Helix: -- Pleated Sheets
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MOLECULAR STRUCTURE TERTIARY 3-D shape
Globular – (round clusters – hemoglobin) Fibrous – (long threads – collegen) Hydrophobic interaction – nonpolar sections of molecule clump to middle of protein away from any possible sources of water
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MOLECULAR STRUCTURE QUATERNARY
Interaction of multiple polypeptide chains
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ENZYMES Substrate – substance being broken down
Active site – area where substrate/enzyme connect Induced Fit – slight change of shape as enzyme & substrate join
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Affects on Reaction Rates
Cofactors / coenzymes – an additional enzyme working on same substrate Competitive Inhibitors – block active site
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Affects on Reaction Rates
Noncompetitive Inhibitors – changes shape of the enzyme without attaching to the active site Allosteric regulation – attachment of another molecule which changes the shape of the enzyme
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Metabolic Controls Feedback Inhibition – the product of the reaction binds to the enzyme & prevents it from doing its job. Avoid excess production
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Metabolic Controls Cooperativity – (form allosteric regulation) when another molecule helps maintain shape of enzyme
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