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2-19 To investigate the properties of protein-ligand binding at various solution pH values, a biophysical experiment is set up to measure the free energy of bind- ing of these biomolecules. The four states of the protein and ligand are as shown in figure 2.14. Suppose that AG, is found to be -8.0 kcal/mol, and bind AG is found to be -10 kcal/mol at a temperature of 298 K. At a pH of bind 7.5, the apparent equilibrium dissociation constant of the protein-ligand com- plex is determined to be 1.96 × 10~7 M. Given this information, determine the fraction of unbound ligand that is deprotonated at pH 7.5.

2-19 To investigate the properties of protein-ligand binding at various solution pH values, a biophysical experiment is set up to measure the free energy of bind- ing of these biomolecules. The four states of the protein and ligand are as shown in figure 2.14. Suppose that AG, is found to be -8.0 kcal/mol, and bind AG is found to be -10 kcal/mol at a temperature of 298 K. At a pH of bind 7.5, the apparent equilibrium dissociation constant of the protein-ligand com- plex is determined to be 1.96 × 10~7 M. Given this information, determine the fraction of unbound ligand that is deprotonated at pH 7.5.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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2-19 To investigate the properties of protein-ligand binding at various solution pH values, a biophysical experiment is set up to measure the free energy of bind- ing of these biomolecules. The four states of the protein and ligand are as shown in figure 2.14. Suppose that AG, is found to be -8.0 kcal/mol, and bind AG is found to be -10 kcal/mol at a temperature of 298 K. At a pH of bind 7.5, the apparent equilibrium dissociation constant of the protein-ligand com- plex is determined to be 1.96 × 10~7 M. Given this information, determine the fraction of unbound ligand that is deprotonated at pH 7.5.
Transcribed Image Text:2-19 To investigate the properties of protein-ligand binding at various solution pH values, a biophysical experiment is set up to measure the free energy of bind- ing of these biomolecules. The four states of the protein and ligand are as shown in figure 2.14. Suppose that AG, is found to be -8.0 kcal/mol, and bind AG is found to be -10 kcal/mol at a temperature of 298 K. At a pH of bind 7.5, the apparent equilibrium dissociation constant of the protein-ligand com- plex is determined to be 1.96 × 10~7 M. Given this information, determine the fraction of unbound ligand that is deprotonated at pH 7.5.
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