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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Students have asked these similar questions

For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s. a) Calculate the Ks and KM for this reaction. b) Does substrate binding achieve equilibrium or steady state?

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An enzyme lowers the activation energy, (AG) of a reaction from 50.0 kcal/mol to 40.0 kcal/mol. Calulate the catalytic power at 310K. (R-1.987x10 kcal/mol)

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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Chapter 2 Solutions