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bich finalll

Quiz yourself by thinking what should be in each of the black spaces below before clicking on it to display the answer.
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Question
Answer
Keq   =Ka= [H+][A-]/[HA]  
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pKa   = -log(Ka)  
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pH   = -log[H+] = pKa + log([deprotonated]/[protonated])  
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inflection point   where pH=pKa  
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buffer   weak acid + conjugate base  
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dE   = Ef - Ei = Q + W  
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H   = E + PV  
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dG   = dH - TdS = dGo + RTln([p]/[r])  
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R (constant)   0.008314kJ/mol*K  
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avg wt. of an aa   110Da  
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Ramachandran Plot   shows most likely orientation  
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amino acid structure bonds   1: covalent peptide bonds 2: backbone H-bonds 3: interactions of aa sc w/ eachother and backbone atoms 4: weak non-covalent interactions  
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alpha helix   rise/residue=1.5A rise/turn=5.4A residues/turn=3.6 right-handed i to i+4 C=O- - -H-N hydrogen bond  
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beta sheet   antiparallel: one chain -->, other chain <--; straight bonds parallel: both chains -->; diagonal bonds  
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side chain interactions w/ alpha helices   adjacent i to i+3 or i to i+4 pseudo 7 repeat  
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alpha keratin   dimer of a-helices high Cys content -- disulfide bonds 7-residue repeats where a & d are nonpolar coiled coil  
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silk fibroin   antiparellel B-sheets arranged parallel alternating sequence:Gly-X-Gly, X=Ala, Ser all Gly on one side and X on other  
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collagen   basic unit= tropocollagen, 3 left-handed chains interwoven --> right-handed superhelical twist 33% Gly, also some unusual aa's (face center) Pro permits sharp turns covalent x-links between Lys and His diseases: Ehlers-Danlos & brittle bone  
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globular proteins   hydrophilic surface, hydrophobic interior generally all a-helices xor B-sheets supersecondary structures or motifs  
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domains   functionslly independent  
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Created by: jesters
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