BIOCH200 Lecture Notes - Globular Protein, Hydrogen Bond, Valine

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

Document Summary

Bioch 200: protein structure and function (february 7, *it is the hydrophobic interaction that occur within a globular protein that give it its. *structure shape is more fine-tuned via hydrogen bonding, ion pairs (electrostatic interactions), and disulphide bridges (covalent bonds found in cysteine dimers) *domain segment in a polypeptide that has folded into a single functional unit w/ a hydrophobic core (aka functional subregions within a protein ) *motif little folded regions in a protein that is found in other proteins as well (perhaps having the same function) (according to the slide: short region of polypeptide with recognizable 3d shape) example: zinc fingers. *polypeptides have domains because it makes for efficient division of labour: zinc fingers. Brings together cys and his residues to coordinate a zn2+ ion. *prosthetic groups is a part of the tertiary structures of many proteins; is a non- protein component that is permanently bound to it that either provides structure (ex.