The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine) For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.
The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine) For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.
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 distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine)
For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.

Transcribed Image Text:Wild type O, binding curve
Mutant O, binding curve
Wild type CO binding curve
Mutant CO binding curve
Label this axis
Label this axis
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