100 50 2 4 8 10 pH Activity (% of maximal)

Biomedical Instrumentation Systems
1st Edition
ISBN:9781133478294
Author:Chatterjee
Publisher:Chatterjee
Chapter6: Biomedical Electrodes, Sensors, And Transducers
Section: Chapter Questions
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The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state
(protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme shown below?

100
50
2
4
8
10
pH
Activity (% of maximal)
Transcribed Image Text:100 50 2 4 8 10 pH Activity (% of maximal)
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