BIOCH200 Lecture Notes - Lecture 11: Peptide, Proline
4 Oct 2016
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Biochem 200 - lecture #11 - protein structure. Secondary structure: local folding of polypeptide backbone. Allow for h bonding: when each amino acid adopts same geometry, regular secondary structures occur. Maximize: both forms of secondary structure satisfy h bonding potential and steric constraints of polypeptide backbone. Alpha helix: right handed helical structure, carbonyl oxygen forms h bond with nh group 4 spots down. All backbone c=o and n-h are bonded to one another in the helix (except for those at the end: side chains aren"t a part of helical structure but they still play a role in the structure itself. Incompatible patterns of amino acids will usually result in the destabilisation of the helix. Cooh - usually don"t see this side chain back to back; couple of amino acids in between iclicker question: electrostatic repulsions is a reason, because many of those amino acids are mostly negatively charged.
