BIOCH200 Lecture Notes - Amide, Proline, Peptide

• School: University of Alberta
• Department: Biochemistry
• Course: BIOCH200
• Professor: Walter Dixon

Document Summary

Bioch 200 (february 3, 2014) proteins: structure and. Function: primary structure, each protein/polypeptide has its own unique sequence, *peptide bonds are rigid and planar, *electrons are somewhat delocalized (between carboxyl oxygen atom and the amino atom) *seen as a partial double bond that restricts free rotation between c-n bond: *the rotational capabilities are restricted on varying levels depending on that contents or the side chain. Glycine will have far less rotational restrictions than proline: secondary structure, *the way the hydrogen bonds interact will lead to one of two secondary structures. Sheet: h-bond participants in the polypeptide backbone. *amino groups are h-bone donors: secondary structures interact to yield tertiary forms whose structure dictates its function. Grooves in structure present in catalytic proteins: *mutations that change one amino acid into another can cause drastic structural changes to the secondary, tertiary, and quaternary structures. Function may become lost or swapped with a different function.