Two methods that could be applied to the study of hydrogen-deuterium exchange rates in proteins should be mentioned and explained. Concept introduction: Hydrogen-deuterium exchange is a reaction by which a covalently bonded hydrogen atoms are replaced by deuterium atoms. This method is commonly used for the solvent accessibility of proteins and thereby determining the tertiary structure of the protein. The protons on amide groups are exchangeable.

Question

The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S. b Question Content Area The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1. Calculate the catalytic efficiency with S, T, and U. Catalytic efficiency with S = Catalytic efficiency with T = Catalytic efficiency with U = Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?

Answer 1

Question

Chapter 3, Problem 25P

Interpretation Introduction

Interpretation:

Two methods that could be applied to the study of hydrogen-deuterium exchange rates in proteins should be mentioned and explained.

Concept introduction:

Hydrogen-deuterium exchange is a reaction by which a covalently bonded hydrogen atoms are replaced by deuterium atoms. This method is commonly used for the solvent accessibility of proteins and thereby determining the tertiary structure of the protein. The protons on amide groups are exchangeable.

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