The T state of hemoglobin is converted to the R state by what event?Select one:The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently,residues between the alß2 interface.а.b. None of these.The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently,residues between the alß2 interface.С.d.The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently,residues between the alß2 interface.The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently,residues between the alß2 interface.е.

Hemoglobin is a quaternary protein present in the red blood cells (RBC) responsible for the…

Answered: The T state of hemoglobin is converted…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D
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The mutation in hemoglobin at B82 Lys → Asp results in lowered O,-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site (see Figure 7.29; B82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, sug- gest a rationale for the observed reduction in Oz-binding affinity.
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If there was a molecule that causes Hb to be more stable in the T state, this molecule would: a. Generally, raise the affinity of Hb for O2 b. Generally, lower the affinity of Hb for O2 c. Generally, cause Mb to favor the R state while Hb is in the T state d. Generally, cause Hb to dissociate into αβ dimers
The formation of “hard” clots by factor XIIIa involves linking lysine and glutamine side chain residues in fibrin. Draw a representation of the cross-linked product of a reaction between these two amino acids.
A very new Hemoglobin variant, called Hb simplex, has just been identified in patients with hypoxia (i.e. patients for whom the oxygenation of organs is not properly accomplished). However, this variant is able to bind dioxygen with a Kd which is significantly lower to that of Hemoglobin from normal patients. This effect has been associated with the substitution of a Lys by a Met at two distinct sites of the b subunit of Hemoglobin : one site close to the N-terminus, and the other site close to the C-terminus of the polypeptide chain. Most importantly, these 2 sites are known to be involved in the maintain of the physical interactions between the subunits a and b in Hemoglobin. 1) The aforementioned Hb simplex mutations lead to a loss of physical interactions between the subunits a and b. What type(s) of chemical bonds between the 2 subunits (i.e. covalent, electrostatic, ion-dipole, dipole-dipole, van der waals) would you hypothesize to be affected by these mutations? explain. 2)…
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