Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 7, Problem 18P
Interpretation Introduction
Interpretation:
The effect of mutations that placed the
Concept introduction:
The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well.
The process of alteration of DNA sequence or base pair of DNA in a normal gene that forms a mutant gene is known as mutation.
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Hemoglobin variant Yakima contains His rather than Asp at the 99th
description of hemoglobin Yakima.
(Hint! Asp(99)B > His disrupts a H-bond that stabilizes the T state).
position of each B chain (or the 1st position of G helix in B chain). Choose the best
The p50 value of hemoglobin Yakima is lower than p50 of normal hemoglobin.
O B. The p50 value of hemoglobin Yakima is higher than p50 of normal hemoglobin.
The p50 value is not changed in hemoglobin Yakima.
C.
Hemoglobin Yakima will not bind O2
O D.
O E. All of the above
Inducers and Inhibitors of AEP.
Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…
2,3-Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?
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