Consider the dissociation reaction for a protein-ligand complex: P•L P + L A. Sketch a binding curve (fractional saturation 0 vs. ligand concentration [L]) for this protein-ligand complex (ligand A). Show where on that curve you could obtain the dissociation equilibrium constant Ka for the reaction. B. Now sketch on the same axes a 0 vs. [L] plot for a different ligand (B) that binds more weakly than the first ligand. C. Does the weaker binding ligand have a higher, or lower, Ka than the tighter binding ligand?
Consider the dissociation reaction for a protein-ligand complex: P•L P + L A. Sketch a binding curve (fractional saturation 0 vs. ligand concentration [L]) for this protein-ligand complex (ligand A). Show where on that curve you could obtain the dissociation equilibrium constant Ka for the reaction. B. Now sketch on the same axes a 0 vs. [L] plot for a different ligand (B) that binds more weakly than the first ligand. C. Does the weaker binding ligand have a higher, or lower, Ka than the tighter binding ligand?
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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I’m having hard time drawing the graph to answer these questions can you show how to approach them?
![Consider the dissociation reaction for a protein-ligand complex: P•L P + L
A. Sketch a binding curve (fractional saturation 0 vs. ligand concentration [L]) for this protein-ligand
complex (ligand A). Show where on that curve you could obtain the dissociation equilibrium
constant Ka for the reaction.
B. Now sketch on the same axes a 0 vs. [L] plot for a different ligand (B) that binds more weakly
than the first ligand.
C. Does the weaker binding ligand have a higher, or lower, Ka than the tighter binding ligand?
D. Sketch a binding curve for a cooperatively bound ligand with Ko.5 higher than that of Kd for A or
B. (Note: for cooperative binding, each protein molecule would have to have more than 1 binding
site for the ligand; Ko.5 is the experimentally determined ligand concentration that gives 0 = 0.5.)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fb346f182-841a-403a-a24d-d0cded8ee760%2Faa426423-893b-45a1-aa43-d8e77c44211b%2F45hppph_processed.jpeg&w=3840&q=75)
Transcribed Image Text:Consider the dissociation reaction for a protein-ligand complex: P•L P + L
A. Sketch a binding curve (fractional saturation 0 vs. ligand concentration [L]) for this protein-ligand
complex (ligand A). Show where on that curve you could obtain the dissociation equilibrium
constant Ka for the reaction.
B. Now sketch on the same axes a 0 vs. [L] plot for a different ligand (B) that binds more weakly
than the first ligand.
C. Does the weaker binding ligand have a higher, or lower, Ka than the tighter binding ligand?
D. Sketch a binding curve for a cooperatively bound ligand with Ko.5 higher than that of Kd for A or
B. (Note: for cooperative binding, each protein molecule would have to have more than 1 binding
site for the ligand; Ko.5 is the experimentally determined ligand concentration that gives 0 = 0.5.)
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