CHEM150 CH6-8

CHEM150 CH6-8

University

20 Qs

quiz-placeholder

Similar activities

Introduction to Metabolism

Introduction to Metabolism

University

15 Qs

Amino Acids and Proteins Quiz

Amino Acids and Proteins Quiz

University

20 Qs

Chap 16

Chap 16

University

22 Qs

Glucose and Glycogen Metabolism (NUR-1F)

Glucose and Glycogen Metabolism (NUR-1F)

10th Grade - University

15 Qs

UNIT_5_BIOCHEMISTRY_BP203T

UNIT_5_BIOCHEMISTRY_BP203T

University

15 Qs

B1 Exam 1 Practice 1

B1 Exam 1 Practice 1

University

20 Qs

BIMI200 quiz

BIMI200 quiz

University

20 Qs

Chapter 6 Biochemistry

Chapter 6 Biochemistry

University

19 Qs

CHEM150 CH6-8

CHEM150 CH6-8

Assessment

Quiz

Chemistry

University

Hard

Created by

Emilie Hingray

FREE Resource

20 questions

Show all answers

1.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

Where do allosteric effectors bind on an enzyme?

They always bind at the catalytic site.

They always bind at a site different from the catalytic site.

They can bind at either the catalytic site or at a different site.

2.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

In the induced-fit model of substrate binding to enzymes, what happens?

There is a conformational change of the catalytic site when the substrate binds.

There is aggregation of several enzyme molecules when the substrate binds.

The substrate changes its conformation to fit inside the catalytic site.

3.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

What is the main thermodynamics-related difference between a catalyzed and a non-catalyzed reaction?

Both activation energy and net free energy change are null for the catalyzed reaction.

The activation energy change of the catalyzed reaction is the lowest of the 2 reactions.

The net free energy change of the catalyzed reaction is the lowest of the 2 reactions.

4.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

Which of the following is true?

Allosteric enzymes are rarely important in the regulation of metabolic pathways.

Michaelis-Menten kinetics model the mechanism of allosteric enzymes.

An hyperbolic representation of the relation initial velocity vs [S] is a specific characteristic of an allosteric enzyme's behavior.

None of these is true.

5.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

Is hindrate a competitive inhibitor, irreversible inhibitor, or noncompetitive inhibitor?

Competitive inhibitor

Irreversible inhibitor

Noncompetitive inhibitor

6.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

Which of the following types of inhibitor binds reversibly to the enzyme at the same site as the substrate without altering the overall enzyme structure?

Noncompetitive inhibitor

Competitive inhibitor

Irreversible inhibitor

7.

MULTIPLE CHOICE QUESTION

1 min • 1 pt

What does amphipathic mean?

Having both positive and negative charges.

Having both acid and base properties.

Having both hydrophilic and hydrophobic regions.

Having two stereoisomers.

Create a free account and access millions of resources

Create resources
Host any resource
Get auto-graded reports
or continue with
Microsoft
Apple
Others
By signing up, you agree to our Terms of Service & Privacy Policy
Already have an account?