Biochemistry 2280A Lecture Notes - Lecture 4: Protein Structure, Protein Folding, Carboxylic Acid

• School: Western University
• Department: Biochemistry
• Course: Biochemistry 2280A
• Professor: Derek Mc Lachlin

Document Summary

Alpha amino and alpha carboxyl group, its directional, different groups at terminus. Convention when naming amino acid name from n terminus to c terminus. Resonance wihin the molecule created a dipole, with the n and o. Rigidit(cid:455) differs, (cid:272)ause (cid:449)ith dou(cid:271)le (cid:271)o(cid:374)ds it does(cid:374)"t rotate, there is li(cid:373)ited rotation around the bond, so that impacts how proteins fold up. All the atoms in these rectangles, and that all exist on one plane, because there is no rotation of peptide bond. There are bonds that can be rotated whch helps to rotate, a(cid:374)d o(cid:374)es that do(cid:374)"t. The sequence dictates the shape and size of the tertiay, secondary and quaternatry structures. Huge variety, all based on the primary sequence. Central dogma: evolutions acts on the livel of primary structure/sequence! Secondary: folding refer to the structure of backbone atoms. how the backbone folds itself dictates the shape they take. Stabilized by h bonds in the basckbone atoms. 2 types: alpha heli and beta strands.