BCH 2333 Lecture 7: Lecture 7 - Secondary protein structure
8 Feb 2017
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Document Summary
Midterm 1 average was 82% apparently too high so the next midterm will bring it down. 3d is a bit unusual, most organic polymers do not form like this. The native fold has a large number of favourable interactions within the protein. Entropic cost to overcome in folding but can overcome by favourable interactions. Folding is driven by entropy (remember the water molecules and the clathrate cages) Hydrophobic effect = decreases saturation shell volume around hydrophobic groups => val, leu, ile, met, phe, prefer to be interior. Hydrogen bonding = tends to occur on backbone of polypeptide, nh and co, also in between side chains => ser, thr, typ, asp, gln, trp, h bond in the interior of a folded protein. London dispersion forces = van der waals, groups that are packed together. Pseudo double bond in between carbonyl and amine is shorter than a c-n single bond. Biochem page 1 shorter than a c-n single bond.
