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3-423-08ProteinStructure

3-423-08ProteinStructure - phobic ints X X X X Quaternary...

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A relatively small protein Glycine PEPTIDE BOND Condensation Hydrolysis
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A pentapeptide: it has direction… The number of possible different polypeptides of length n amino acids?…20 n Possible dipeptides…400. Possible tripeptides…8000 Ser Gly Tyr Ala Leu Overview of protein structure
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Primary structure (1 o ) -Sequence of AAs -Important bonds/ints = peptide bonds and disulfide bonds (covalent) Secondary (2 o ) -Repeating patterns -Important bonds/ints = H-bonds, vdWaals (noncovalent) Alpha helix ( α -helix) 1 4 X
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X Constraints on α -helices: -steric interferences - too many BIG AA R-groups near each other -electrostatic interferences - several (+) charged R-groups in a row, or (-) (also possible to have attractions) -Prolines -Glycines asp arg Beta ( β ) sheets <------- Constraints on β -sheets: -Long AA R-groups not found
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β -turns: -have prolines, glycines <---- Tertiary structure (3 o ) -the 3-D architecture -Important bonds/ints = hydrophobic ints, H-bonds, vdWaals (noncovalent) (Also, disulfide bonds) H-bonds, Ionic ints X<---Hydro
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Unformatted text preview: phobic ints X X X X Quaternary structure (4 o )-Only in proteins with more than one polypeptide subunit-Important bonds/ints = hydrophobic ints, H-bonds, ionic ints (mostly noncovalent)… …but, there are some multisubunit proteins that have covalent bonds between subunits Not all proteins have 2 o structure… But there are proteins with lots of 2 o structure… Ex: Collagen: skin, bone, tendon, cartilage,teeth 1 o structure = Gly every 3rd residue, lots of Pro and Hydroxyproline residues. 2 o structure = tight helix (COLLAGEN helix, not alpha) Not all proteins have 4 o structure…-triple collagen helix (not α )-Glycine is every 3rd residue (only one that will fit in the center of triple helix) Alterations in 1 o structure can alter final functional protein structure, function Example: Collagen-Glycine-Proline, Hydroxyproline (Scurvy, vitamin C, prolyl hydroxylase) Denaturation, renaturaton, protein folding...
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