Please briefly explain your answer. Thank You! l. A new hemoglobin variant (we w
ID: 488500 • Letter: P
Question
Please briefly explain your answer. Thank You! l. A new hemoglobin variant (we will dub as a mutant Hb) was discovered in a remote population. The oxygen binding curve is shown below (curve 1 is wild-type; curve 2 is mutant Hb). The Hill coefficient is identical to the wild-type, and the mutant Hb shows a slightly weaker response to pH compared with the wild-type. This mutant hemoglobin can be considered (circle one) a high oxygen affinity protein a low oxygen J affinity protein Which state is more stable? T state Partial Pressure oroxmem (kPa) R state This mutation can most likely be found at in heme pocket 1-2 interface 1-1 interface the BPG binding pocket Explain your answer! Show the oxygen binding curve for the the mutant Hb with a drop in pH on the curve, labeling it 3. 2. The argument that there is overall retention of the stereochemistry of ring D of the NAG-NAM hexamer when clipped by lysozyme is a pro-SN2 argument. Some scientists believe that if you invoke the argument of electrostatic catalysis you can successfully argue that the mechanism is S 1. Explain
Explanation / Answer
The protease that use general acid base catalysis is serine protease. The serine protease is an enzyme that catalyses the hydrolysis of peptide bonds with an active site serene residue that acts as a nucleophile during catalysis.
The protease that use electrostatic catalysis is serine protease.
The protease that use covalent catalysis is serine protease and cysteine protase. The essential step in covalent catalysis is creating covalent intermediate. A covalent intermediate encourages the reaction along to the transition state, which then in turn is used to speed up the reaction.