Which of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition.When two proteins form a complex there is an unfavorable loss of rotational-translational entropy.Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy.The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins.Burial of an uncompensated positive charge inside proteins is usually unfavorable.So-called van der Waals’ interactions are essentially electrostatic in origin.Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding.Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.

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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

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Which of the following statements are true?

Electrostatic interactions are the dominant forces in protein molecular recognition.
When two proteins form a complex there is an unfavorable loss of rotational-translational entropy.
Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy.
The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins.
Burial of an uncompensated positive charge inside proteins is usually unfavorable.
So-called van der Waals’ interactions are essentially electrostatic in origin.
Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding.
Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.

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