The catalytic activity of an enzyme is being measured at pH 7.5 and requires that the side chain of a specific Cys (C) residue be in its unprotonated (conjugate base) form for the enzyme to be active. That specific Cys side chain in the protein has a pka of 7.8. a) For this Cys side chain with a pKa of 7.8, what is the base/acid ratio at pH 7.5? b) What fraction of the total enzyme molecules in a solution of the enzyme at pH 7.5 have that Cys side chain in the active form? (Express the answer as a %) c) The name of the Cys side chain functional group is? d) The active form of the Cys side chain in this enzyme would be? i. positively (+) charged ii. uncharged (neutral) iii. negatively (–) charged
The catalytic activity of an enzyme is being measured at pH 7.5 and requires that the side chain of a specific Cys (C) residue be in its unprotonated (conjugate base) form for the enzyme to be active. That specific Cys side chain in the protein has a pka of 7.8. a) For this Cys side chain with a pKa of 7.8, what is the base/acid ratio at pH 7.5? b) What fraction of the total enzyme molecules in a solution of the enzyme at pH 7.5 have that Cys side chain in the active form? (Express the answer as a %) c) The name of the Cys side chain functional group is? d) The active form of the Cys side chain in this enzyme would be? i. positively (+) charged ii. uncharged (neutral) iii. negatively (–) charged
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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