Role of urea in denaturing the proteins. Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

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Answer 1

Question

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.

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Answer 2

Question

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.

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Answer 3

Question

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.

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Answer 4

Question

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.

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Answer 5

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.

Answer 6

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.

Answer 7

Chapter 4, Problem 1Q

Summary Introduction

To explain: Role of urea in denaturing the proteins.

Introduction: A long chain of amino-acids joined by peptide bond is known as proteins. The physical or chemical agents that can be used to stimulate the unfolding of the polypeptide chain are called denaturants. Urea is an important denaturant used to denature the proteins.

Answer 8

Expert Solution & Answer

Explanation of Solution

Urea is an organic compound generally used for protein denaturation. It has the ability to form hydrogen bonds. It can act as a hydrogen bond acceptor due to its –C=O group and as a hydrogen bond donor due to its –NH2 group. Urea forms intermolecular hydrogen bonding between amino-acids, thus disrupting the normal protein folding and changing it into a different conformation. Also, it fits in between the hydrogen bonds which stabilize the protein, thus destabilizing the original protein structure. When the concentration of the urea is high, the hydrogen bond network of water molecules with protein would get disrupted. The hydrophobic interactions that help to keep up the secondary and tertiary structure of the proteins would be suppressed by the urea as well.