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.

Question

Want to see more full solutions like this?

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

Students have asked these similar questions

JOB UPDATE Apply on- COMPANY Vinkjobs.com @ OR Search "VinkJobs.com" on Google JOB PROFILE JOB LOCATION ACCENTURE APPLICATION DEVELOPMENT MULTIPLE CITIES HITACHI FULL STACK DEV BENGALURU PAYU BUSINESS ANALYST MULTIPLE CITIES MEESHO DATA SCIENTIST BENGALURU ORACLE SOFTWARE ENGINEER BENGALURU LUMEL FRONT END DEVELOPER CHENNAI MPHASIS INKLE TECH SUPPORT ENGINEER BENGALURU CUSTOMER SUPPORT BENGALURU MAKE MY TRIP KEY ACCOUNT MANAGER AMAZON DATA ASSOCIATE DELHI NCR BENGALURU

stripe.perplexity.ai/p + ← Return to Perplexity Al, Inc perplexity CURRENT SUBSCRIPTION 13 13 Perplexity Pro $0.00 per month View details Your subscription ends on January 28, 2026.

You’ve isolated a protein and determined that the Native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD. The enzyme was found to be 0.829% NAD (by weight). What further can be said regarding the structure of the polypeptide?

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

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

Want to see more full solutions like this?

Chapter 2 Solutions