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Which of the following must be true based on the data below for ligand L binding to protein A and to protein B? Choice 1 of 4:Protein A binds at least 2 molecules of ligand L. Choice 2 of 4:The Kd for ligand binding to B is approximately 4 micromolar. Choice 3 of 4:When exposed to ligand L, protein A reaches maximal binding faster than does protein B. Choice 4 of 4:Protein B must adopt at least 2 different conformations with different binding affinities.

Which of the following must be true based on the data below for ligand L binding to protein A and to protein B? Choice 1 of 4:Protein A binds at least 2 molecules of ligand L. Choice 2 of 4:The Kd for ligand binding to B is approximately 4 micromolar. Choice 3 of 4:When exposed to ligand L, protein A reaches maximal binding faster than does protein B. Choice 4 of 4:Protein B must adopt at least 2 different conformations with different binding affinities.

Biochemistry
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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Which of the following must be true based on the data below for ligand L binding to protein A and to protein B?

Choice 1 of 4:Protein A binds at least 2 molecules of ligand L.
Choice 2 of 4:The Kd for ligand binding to B is approximately 4 micromolar.
Choice 3 of 4:When exposed to ligand L, protein A reaches maximal binding faster than does protein B.
Choice 4 of 4:Protein B must adopt at least 2 different conformations with different binding affinities.
The image is a graph illustrating the relationship between ligand concentration and the fraction of ligand bound for two different samples, labeled A and B. ### Graph Details: - **X-axis (Horizontal):** Represents the Ligand Concentration in micromolar (μM), ranging from 0 to 14. - **Y-axis (Vertical):** Represents the Fraction Bound, a unitless measure ranging from 0 to 1. - **Data Series:** - **Sample A:** Indicated by dark circles and a dark line. It shows a rapid increase in the fraction bound as ligand concentration increases, reaching a plateau near a fraction bound of 1. - **Sample B:** Indicated by light squares and a light line. It shows a more gradual increase in the fraction bound with a similar plateau slightly below 1. ### Observations: - Both samples A and B exhibit a typical binding curve pattern, with the fraction bound increasing as ligand concentration increases until saturation is reached. - Sample A binds more rapidly than Sample B, achieving a higher fraction bound at lower ligand concentrations. This type of graph is commonly used in biochemical studies to illustrate the binding affinity of ligands to proteins or other molecules, where a higher and faster fraction bound indicates stronger binding affinity.
Transcribed Image Text:The image is a graph illustrating the relationship between ligand concentration and the fraction of ligand bound for two different samples, labeled A and B. ### Graph Details: - **X-axis (Horizontal):** Represents the Ligand Concentration in micromolar (μM), ranging from 0 to 14. - **Y-axis (Vertical):** Represents the Fraction Bound, a unitless measure ranging from 0 to 1. - **Data Series:** - **Sample A:** Indicated by dark circles and a dark line. It shows a rapid increase in the fraction bound as ligand concentration increases, reaching a plateau near a fraction bound of 1. - **Sample B:** Indicated by light squares and a light line. It shows a more gradual increase in the fraction bound with a similar plateau slightly below 1. ### Observations: - Both samples A and B exhibit a typical binding curve pattern, with the fraction bound increasing as ligand concentration increases until saturation is reached. - Sample A binds more rapidly than Sample B, achieving a higher fraction bound at lower ligand concentrations. This type of graph is commonly used in biochemical studies to illustrate the binding affinity of ligands to proteins or other molecules, where a higher and faster fraction bound indicates stronger binding affinity.
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