bich finalll
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
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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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