The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base. Introduction: Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

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Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

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Answer 2

Question

Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

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Answer 3

Question

Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

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Answer 4

Question

Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

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Answer 5

Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

Answer 6

Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

Answer 7

Chapter 6, Problem 79TQ

Summary Introduction

To review:

The process throughwhich the carboxylic group of the aspartate activates the nitrogen of histidine to make it a stronger base.

Introduction:

Histidine and aspartate are typical components of the catalytic triads present in most serine proteases. A characteristic example of serine proteases is chymotrypsin, which is composed of aspartate at position 102, histidine at 57, and serine at 195. There are various inhibitors that affect the catalytic activity of this triad.

Answer 8

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Answer 11

Ch. 6 - Prob. 1Q Ch. 6 - Prob. 2Q Ch. 6 - Prob. 3Q Ch. 6 - Prob. 4Q Ch. 6 - Prob. 5Q Ch. 6 - Prob. 6Q Ch. 6 - Prob. 7Q Ch. 6 - Prob. 8Q Ch. 6 - Prob. 9Q Ch. 6 - Prob. 1RQ

Solution Summary: The author analyzes how the carboxylic group of aspartate activates the nitrogen of histidine to make it a stronger base.

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