BCH 2333 Lecture 2: Biochemistry Note 2
18 Oct 2016
School
Department
Course
Professor
Document Summary
Need at least two for a quaternary structure. Polystyrene or nylon which have random 3d shape. This 3d structure is called the native fold. The native fold has a large number of favorable interactions within the protein. Entopic cost must be overcome by favorable interactions for protein to fold. Hydrophobic effect: when we have hydrophobic molecules that aggregate in water to decrease solvation shell volume around the hydrophobic groups. Important part of stabilizing proteins. (val, leu, ile, met, phe). Important part that proteins do is stick on the side chains inside proteins where there is no water. Hydrogen bonds: amide backbone are essential (nh and co). Asp, gln, trp all h-bond on interior of protein). Packing density in drop of oil = 0. 6, typical crystal = 0. 7, typical protein 0. 75. This resonance structure has a huge impact on biochemistry. Amide c-n bond does not rotate freely because the carbonyl and the nh are all in one plane.
