A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit willmost likely result inNot enough informationHigher than normal binding affinity to oxygenLower than normal binding affinity to oxygenNormal binding to oxygen

Changing the genetic code of a living thing permanently and inherited is known as a mutation. The…

Answered: A mutation of Lysine 82 (in the…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 22P

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Assume that a new oxygen transport protein has been discovered in certaininvertebrate animals. X-ray diffraction of the deoxy protein reveals that ithas the dimeric structure shown in panel (a) of the accompanying figure,with a salt bridge between residues histidine 13 and aspartic acid 85. Thetwo monomers interact by salt bridges between the C- and N-termini. TheO2-binding site lies between the two iron atoms shown, which are rigidlylinked to helices A and C (see panel (b)). In the deoxy form, the spacebetween the iron atoms is too small to hold O2, and so the Fe atoms must be forced apart when O2 is bound.Answer the following questions, explaining your answer in each case interms of the structure shown below.(a) Is this molecule likely to show cooperative oxygen binding?(b) Is this molecule likely to exhibit a Bohr effect?(c) Predict the likely effect of a mutation that replaced aspartic acid 85 bya lysine residue.
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A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in Not enough information Higher than normal binding affinity to oxygen Lower than normal binding affinity to oxygen Normal binding to oxygen