BCHS 3304- Final Exam Guide - Comprehensive Notes for the exam ( 22 pages long!)
Document Summary
Chapter 6 textbook notes: secondary structure. Random coil totally disordered and rapidly fluctuating conformations assumed by denatured (fully unfolded) proteins in solution. Native (folded) proteins non-repetitive structures are no less ordered than are helices or sheets; they are simply irregular more difficult to describe. Variations in a. a. sequence/overall structure of the folded protein can distort the regular conformation of secondary structural elements ( (cid:271)ulge, heli(cid:454) (cid:272)appi(cid:374)g (cid:895: tertiary structure. X-ray crystallography technique that directly images molecules. Nmr yields additional peaks arising from the interactions of protons that are less than 5a apart. Polar side chains extend toward protein surface help form protein surface. Nonpolar side chains largely expand towards interior occupy interior. In some multidomain proteins, binding sites occupy the clefts between domains covalent connection between domains allows flexible interactions between the protein and the small molecule. Quaternary structure spatial arrangement of polypeptide subunits.
