Although all of these play a part, the most important factor which drives protein folding is: a) hydrogen bond formation b) salt bridge formation c) ion-dipole interactions d) the hydrophobic effect The active site of an enzyme binds which type of molecule? a) allosteric activator b) coenzyme c) substrate d) product A coenzyme is also considered to be a prosthetic group if it: a) assists in enzyme catalysis b) binds to the active site c) acts as an allosteric inhibitor d) is covalently bound to the enzyme Proteases catalyze the cleavage of proteins into smaller peptides and amino acids by reaction with water. Proteases fall into the broader class of: a) transferases b) lyases c) hydrolases d) oxidoreductases 13. The Michaelis - Menten constant Km represents: a) 1/2 Vmax b) the substrate concentration at 1/2 Vmax c) 1/2 the substrate concentration at Vmax d) the minimum amount of substrate needed to initiate the reaction Enzymes alter which of these thermodynamic parameters? a) enthalpy b) entropy c) Gibbs free energy d) activation energy Suicide inhibitors exert their action by: a) reacting with cofactors and coenzymes b) causing enzyme denaturation c) forming a strong covalent bond to the active site d) cleaving specific peptide bonds which render the enzyme inactive
Although all of these play a part, the most important factor which drives protein folding is: a) hydrogen bond formation b) salt bridge formation c) ion-dipole interactions d) the hydrophobic effect The active site of an enzyme binds which type of molecule? a) allosteric activator b) coenzyme c) substrate d) product A coenzyme is also considered to be a prosthetic group if it: a) assists in enzyme catalysis b) binds to the active site c) acts as an allosteric inhibitor d) is covalently bound to the enzyme Proteases catalyze the cleavage of proteins into smaller peptides and amino acids by reaction with water. Proteases fall into the broader class of: a) transferases b) lyases c) hydrolases d) oxidoreductases 13. The Michaelis - Menten constant Km represents: a) 1/2 Vmax b) the substrate concentration at 1/2 Vmax c) 1/2 the substrate concentration at Vmax d) the minimum amount of substrate needed to initiate the reaction Enzymes alter which of these thermodynamic parameters? a) enthalpy b) entropy c) Gibbs free energy d) activation energy Suicide inhibitors exert their action by: a) reacting with cofactors and coenzymes b) causing enzyme denaturation c) forming a strong covalent bond to the active site d) cleaving specific peptide bonds which render the enzyme inactive
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
Related questions
Question
- Although all of these play a part, the most important factor which drives protein folding is: a) hydrogen bond formation b) salt bridge formation c) ion-dipole interactions d) the hydrophobic effect
- The active site of an enzyme binds which type of molecule? a) allosteric activator b) coenzyme c) substrate d) product
- A coenzyme is also considered to be a prosthetic group if it: a) assists in enzyme catalysis b) binds to the active site c) acts as an allosteric inhibitor d) is covalently bound to the enzyme
- Proteases catalyze the cleavage of proteins into smaller peptides and amino acids by reaction with water. Proteases fall into the broader class of: a) transferases b) lyases c) hydrolases d) oxidoreductases
13. The Michaelis - Menten constant Km represents: a) 1/2 Vmax b) the substrate concentration at 1/2 Vmax c) 1/2 the substrate concentration at Vmax d) the minimum amount of substrate needed to initiate the reaction
- Enzymes alter which of these
thermodynamic parameters? a) enthalpy b) entropy c) Gibbs free energy d) activation energy - Suicide inhibitors exert their action by: a) reacting with cofactors and coenzymes b) causing enzyme denaturation c) forming a strong covalent bond to the active site d) cleaving specific peptide bonds which render the enzyme inactive
AI-Generated Solution
Unlock instant AI solutions
Tap the button
to generate a solution
Recommended textbooks for you

Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman

Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY

Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman

Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY

Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning

Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning

Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON