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bich finalll

QuestionAnswer
Keq =Ka= [H+][A-]/[HA]
pKa = -log(Ka)
pH = -log[H+] = pKa + log([deprotonated]/[protonated])
inflection point where pH=pKa
buffer weak acid + conjugate base
dE = Ef - Ei = Q + W
H = E + PV
dG = dH - TdS = dGo + RTln([p]/[r])
R (constant) 0.008314kJ/mol*K
avg wt. of an aa 110Da
Ramachandran Plot shows most likely orientation
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
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
beta sheet antiparallel: one chain -->, other chain <--; straight bonds parallel: both chains -->; diagonal bonds
side chain interactions w/ alpha helices adjacent i to i+3 or i to i+4 pseudo 7 repeat
alpha keratin dimer of a-helices high Cys content -- disulfide bonds 7-residue repeats where a & d are nonpolar coiled coil
silk fibroin antiparellel B-sheets arranged parallel alternating sequence:Gly-X-Gly, X=Ala, Ser all Gly on one side and X on other
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
globular proteins hydrophilic surface, hydrophobic interior generally all a-helices xor B-sheets supersecondary structures or motifs
domains functionslly independent
Created by: Jessica S Jessica S on 2012-12-06



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