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An antibody (Ab) can bìnd to its antigen binding site (B) with a high affinity (large negative AG°). The antibody and the antigen are mixed at low concentrations and allowed to reach equilibrium. The concentrations measured are [Ab] = 1 nM, [B] = 40 %3D nM, and [Ab-B] = 30 nM, for the equilibrium Ab +B=Ab-B. Imagine that this binding were due entirely to hydrogen bonds. Referring to question 3C above, how many hydrogen bonds would form between Ab and B upon binding? If you were going to manufacture a coronavirus test kit with an antibody that tightly binds to an antigen found in the virus, would you want the antibody/antigen binding to have a Ka in the nM, µM, or mM range? Why?

An antibody (Ab) can bìnd to its antigen binding site (B) with a high affinity (large negative AG°). The antibody and the antigen are mixed at low concentrations and allowed to reach equilibrium. The concentrations measured are [Ab] = 1 nM, [B] = 40 %3D nM, and [Ab-B] = 30 nM, for the equilibrium Ab +B=Ab-B. Imagine that this binding were due entirely to hydrogen bonds. Referring to question 3C above, how many hydrogen bonds would form between Ab and B upon binding? If you were going to manufacture a coronavirus test kit with an antibody that tightly binds to an antigen found in the virus, would you want the antibody/antigen binding to have a Ka in the nM, µM, or mM range? Why?

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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An antibody (Ab) can bind to its antigen binding site (B) with a high affinity (large negative AGO). The antibody and the antigen are mixed at low concentrations and allowed to reach equilibrium. The concentrations measured are [Ab] = 1 nM, [B] = 40 nM, and [Ab-B] = 30 nM, for the equilibrium Ab + B= Ab-B. Imagine that this binding were due entirely to hydrogen bonds. Referring to question 3C above, how many hydrogen bonds would form between Ab and B upon binding? If you were going to manufacture a coronavirus test kit with an antibody that tightly binds to an antigen found in the virus, would you want the antibody/antigen binding to have a Ka in the nM, µM, or mM range? Why?
Transcribed Image Text:An antibody (Ab) can bind to its antigen binding site (B) with a high affinity (large negative AGO). The antibody and the antigen are mixed at low concentrations and allowed to reach equilibrium. The concentrations measured are [Ab] = 1 nM, [B] = 40 nM, and [Ab-B] = 30 nM, for the equilibrium Ab + B= Ab-B. Imagine that this binding were due entirely to hydrogen bonds. Referring to question 3C above, how many hydrogen bonds would form between Ab and B upon binding? If you were going to manufacture a coronavirus test kit with an antibody that tightly binds to an antigen found in the virus, would you want the antibody/antigen binding to have a Ka in the nM, µM, or mM range? Why?
A common unit of energy useful for biochemical calculations is kgT, which is the product of Boltzmann's constant (kg = 1.38 x 10-23 J/K) and absolute temperature (T). Note that this quantity of energy is close to the average kinetic energy of a molecule at temperature T (actually 3/2 kgT). C. What is the strength of a hydrogen bond in water in units of kgT/molecule? Hydrogen bonds can vary in strength (e.g., linear vs. bent), but for this problem let's say the bond strength is 6 kJ/mol.
Transcribed Image Text:A common unit of energy useful for biochemical calculations is kgT, which is the product of Boltzmann's constant (kg = 1.38 x 10-23 J/K) and absolute temperature (T). Note that this quantity of energy is close to the average kinetic energy of a molecule at temperature T (actually 3/2 kgT). C. What is the strength of a hydrogen bond in water in units of kgT/molecule? Hydrogen bonds can vary in strength (e.g., linear vs. bent), but for this problem let's say the bond strength is 6 kJ/mol.
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The antibodies bind to its antigen via non n covalent interactions like hydrogen bonding, hydrophobic interactions and van der waals interaction. The dissociation Kd is the concentration of ligand at which half the ligand binding sites on the protein are occupied in a system residing in equilibrium. The dissociation Kd and affinity are between Antibody and antigen are inversely related. 

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