Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified. Concept introduction: Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin. Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine. Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan. To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

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Answer 1

Question

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

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Answer 2

Question

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

Expert Solution & Answer

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Answer 3

Question

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

Expert Solution & Answer

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Answer 4

Question

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

Expert Solution & Answer

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Answer 5

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

Answer 6

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

Answer 7

Chapter 25.5, Problem 33ATS

Interpretation Introduction

Interpretation:

Cleavage of the given cyclopeptide by trypsin and chymotrypsin gives the same fragments or not need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To explain : To explain whether the fragments obtained by hydrolysis of cyclopeptide using trypsin and chymotrypsin are same or different.

Answer 8

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Answer 9

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Answer 10

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Answer 11

Ch. 25.2 - Prob. 1CC Ch. 25.2 - Prob. 2CC Ch. 25.2 - Prob. 3CC Ch. 25.2 - Prob. 1LTS Ch. 25.2 - Prob. 4PTS Ch. 25.2 - Prob. 5ATS Ch. 25.2 - Prob. 6ATS Ch. 25.2 - Prob. 7CC Ch. 25.2 - Prob. 8CC Ch. 25.2 - Prob. 9CC

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Chapter 25 Solutions