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 elastase to selectively cleave? Choose the best option from those provided. Chymotrypsin ala arg asn asp Asp 189. Asp 189 Trypsin Val 190 Val 216 Val 216 Val 190 Elastase

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Chapter1: Chemical Foundations
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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 elastase to selectively cleave? Choose the best option from those
provided.
Chymotrypsin
ala
arg
asn
asp
Asp 189-
Asp 189
Trypsin
Val 190
Val 216
Val 216 Val 190
Elastase
Transcribed Image Text: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 elastase to selectively cleave? Choose the best option from those provided. Chymotrypsin ala arg asn asp Asp 189- Asp 189 Trypsin Val 190 Val 216 Val 216 Val 190 Elastase
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