The explanation for the increase in the p K a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad. Introduction: A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

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Answer 1

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Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

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Answer 2

Question

Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

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Answer 3

Question

Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

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Answer 4

Question

Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

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Answer 5

Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

Answer 6

Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

Answer 7

Chapter 6, Problem 71TQ

Summary Introduction

To review:

The explanation for the increase in the p K_a of histidine due to the proximity of an aspartate carboxylate group to the imidazole group of histidine in a serine protease triad.

Introduction:

A serine protease triad is referred to as the protease that catalyzes the hydrolysis of the peptide bond of serine. It is found in the active site of most enzyme, such aschymotrypsin. This triad, as the name suggests, contains three amino acid residues of aspartate, histidin, end serine. It forms the class of hydrolases due to its function.

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 describes the serine protease triad, which catalyzes the hydrolysis of the peptide bond of Serine. It contains three amino acid residues of aspartate, histidin

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