Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water. Introduction : The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

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Answer 1

Question

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

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At a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a net charge of zero, but the predominant form of alanine at its pl is zwitterionic. CH3 H,N CH3 ** H¸N-C H Zwitterionic H Uncharged OH Select statements that explain why alanine is predominantly zwitterionic at its pl. pk of alanine's amino group is more than its pl. pk of alanine's carboxyl group is more than its pl. PK of alanine's carboxyl group is less than its pl. pk of alanine's amino group is less than its pl. Correct Answer What fraction of alanine is in the completely uncharged form at its pl? 1 in 2.2 × 107 1 in 1.6 × 10² 1 in 4680 1 in 9460

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Answer 2

Question

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

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Answer 3

Question

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

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Answer 4

Question

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

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Answer 5

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

Answer 6

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

Answer 7

Chapter 2, Problem 1P

Summary Introduction

To determine: Whether the ionic interaction between the enzyme and substrate are stronger or weaker if the ATP-binding site of an enzyme is buried in the interior of the enzyme in a hydrophobic environment than the same interaction on the surface of the enzyme when exposed to water.

Introduction:

The ionic bonding results from the interaction of ionic species. The ionic bonding forms the hydrophilic compounds. The hydrophilic compounds are more likely to be dissolved in water than the hydrophobic compounds. There is binding between the enzyme and substrate.

Answer 8

Expert Solution & Answer

Explanation of Solution

Explanation:

The ionic forces are proportional to an inverse of dielectric constant. The dielectric constant (ε_r) of water is 78.54 at 25 °C. This value accounts for less strong forces of attraction. The ionic forces between substrate and enzyme will be weaker if they both are present in water. This will affect the binding of enzyme to substrate.

The inner portion of protein is hydrophobic and the dielectric constant is lower in the hydrophobic regions. The ionic forces of attraction between enzyme and substrate in core of protein will be stronger and the substrate and enzyme will bind to each other effectively.

Therefore, the ionic forces of attraction will be stronger, if the ATP binding site present in the core of protein than the forces of attraction, if the binding site is exposed to water.

Answer 9

Expert Solution & Answer

Answer 10

Expert Solution & Answer

Answer 11

Ch. 2 - Prob. 1P Ch. 2 - Prob. 2P Ch. 2 - Prob. 3P Ch. 2 - Prob. 4P Ch. 2 - Prob. 5P Ch. 2 - Prob. 6P Ch. 2 - Prob. 7P Ch. 2 - Prob. 8P Ch. 2 - Prob. 9P Ch. 2 - Prob. 10P

Explanation of Solution

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