The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1- ( p-toluenesulfonyl ) -amido-2-phenylethylchloromethyl ketone has to be determined. Concept Introduction: Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine. The binding site of chymotrypsin is illustrated as follows:

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Answer 1

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Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

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Answer 2

Question

Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

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Answer 3

Question

Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

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Answer 4

Question

Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

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Answer 5

Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

Answer 6

Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

Answer 7

Chapter 19, Problem 9MCP

Interpretation Introduction

Interpretation:

The reason behind the selective inhibition of chymotrypsin and not trypsin by L-1-(p-toluenesulfonyl)-amido-2-phenylethylchloromethyl ketone has to be determined.

Concept Introduction:

Chymotrypsin cleaves at the carboxyl-terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Trypsin cleaves at the carboxyl-terminal of positively charged amino acid lysine and arginine.

The binding site of chymotrypsin is illustrated as follows:

Answer 8

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Answer 11

Ch. 19.8 - Prob. 19.12Q Ch. 19.10 - Prob. 19.13Q Ch. 19.10 - Prob. 19.14Q Ch. 19.10 - Prob. 19.15Q Ch. 19.10 - Prob. 19.16Q Ch. 19.11 - Prob. 19.17Q Ch. 19.11 - Prob. 19.18Q Ch. 19.11 - Prob. 19.19Q Ch. 19.11 - Prob. 19.20Q Ch. 19 - Prob. 19.21QP

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