The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given. Concept introduction: Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal). Endopeptidases cleave peptide bonds that are not at the end. Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine. Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp. Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

Question

Want to see the full answer?

Answer 1

Question

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

* Hint: Think back to Chem 1 solubility rules. Follow Up Questions for Part B 12. What impact do the following disturbances to a system at equilibrium have on k, the rate constant for the forward reaction? Explain. (4 pts) a) Changing the concentration of a reactant or product. (2 pts) b) Changing the temperature of an exothermic reaction. (2 pts) of

Draw TWO general chemical equation to prepare Symmetrical and non-Symmetrical ethers Draw 1 chemical reaction of an ether

Please help me with the following questions for chemistry.

Answer 2

Question

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 5

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Answer 6

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

Answer 7

Chapter 17, Problem 55P

(a)

Interpretation Introduction

Interpretation:

The fragments obtained from the cleavage of given peptide chain by trypsin, cyanogen bromide and chymotrypsin should be given.

Concept introduction:

Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).

Endopeptidases cleave peptide bonds that are not at the end.

Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.

Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain aromatic six-membered rings such as Phe, Tyr and Trp.

Cyanogen bromide cleaves the C-terminal peptide of Methionine in a peptide chain.

Answer 8

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Answer 9

(b)

Interpretation Introduction

Interpretation:

The numbers of primary structure if the amino acids contained in each fragment are known has to be determined.

Concept introduction:

The number of primary structures in a polypeptide is determined by checking the number of disulfide bridges connected with primary structures.

Disulfide bridges are formed between thiol groups of cysteine.

Answer 10

Expert Solution & Answer

Answer 11

Expert Solution & Answer

Answer 12

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 13

Ch. 17.1 - a. Explain why, when the imidazole ring of...Ch. 17.2 - Prob. 2P Ch. 17.3 - Prob. 3P Ch. 17.3 - Prob. 4P Ch. 17.3 - Prob. 6P Ch. 17.4 - Calculate the pI of each of the following amino...Ch. 17.4 - a. Which amino acid has the lowest pI value? b....Ch. 17.5 - What aldehyde is formed when valine is treated...Ch. 17.5 - Prob. 10P Ch. 17.5 - Prob. 11P

Solution Summary: The author explains how endopeptidases cleave peptide bonds that are not at the end.

Concept explainers

Videos

Want to see the full answer?

Chapter 17 Solutions