BCH 3125 Lecture Notes - Lecture 8: High-Performance Liquid Chromatography, Acid Dissociation Constant, Protein Structure
30 Aug 2019
School
Department
Course
Professor
Document Summary
Polymerization of hbs into fibres: mutation of glu (neg. charge) to val (hydrophobic) Fit into hydrophobic pocket, forming dimers: low [o2] Conformational upon binding o2 that hides binding pocket. The native structure of a protein is determined by their amino acid sequence: pka and polarity dictate side chain chemistry which determines protein structure. Side chain chemistry (pka: environment dependent / if protein changes conformation to make it closer to another a. a. If near (-) charged a. a, stabilize protonated form and shift pka to higher ph so it holds onto proton stronger than in aq. If near neutral a. a, stabilize neutral form and shift pka to lower ph, so it give up proton more easily than in aq. Solution: pka = ph: 50% protonated, 50% deprotonated. Raise ph and lower [h+] to favour deprotonated / neutral form ph > pka = deprotonate: measured. Based on relative portioning between aqueous and organic phase. Polar = affinity for aqueous phase over organic.
