We talked in class about how the active site (specifically the "deep, hydrophobic pocket") accounts for the specificity of the peptide bonds that are cleaved by chymotrypsin. Below is a figure that shows the active site for two other serine proteases, trypsin and elastase. Based on the information provided, at what C-terminus would you expect trypsin to selectively cleave? Choose the best option from those provided.. Bego Chymotrypsin ala arg asp glu Asp 189- Asp 189 Trypsin Val 190 Val 216 Val 216 Val 190 Elastase

We talked in class about how the active site (specifically the "deep, hydrophobic pocket") accounts for the specificity of the peptide bonds that are cleaved by chymotrypsin. Below is a figure that shows the active site for two other serine proteases, trypsin and elastase. Based on the information provided, at what C-terminus would you expect trypsin to selectively cleave? Choose the best option from those provided.. Bego Chymotrypsin ala arg asp glu Asp 189- Asp 189 Trypsin Val 190 Val 216 Val 216 Val 190 Elastase

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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Question

We talked in class about how the active site (specifically the "deep, hydrophobic
pocket") accounts for the specificity of the peptide bonds that are cleaved by
chymotrypsin.
Below is a figure that shows the active site for two other serine proteases, trypsin
and elastase. Based on the information provided, at what C-terminus would you
expect trypsin to selectively cleave? Choose the best option from those
provided..
Chymotrypsin
ala
arg
asp
glu
gin
Asp 189-
Asp 189
Trypsin
Val 190
Val 216
Val 216
Val 190
Elastase

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