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Solvent-induced interactions and forces in protein foldinghydrophobic-hydrophilic phenomena /

Record Type:	Electronic resources : Monograph/item
Title/Author:	Solvent-induced interactions and forces in protein foldingby Arieh Ben-Naim.
Reminder of title:	hydrophobic-hydrophilic phenomena /
Author:	Ben-Naim, Arieh.
Published:	Cham :Springer Nature Switzerland :2023.
Description:	xiii, 174 p. :ill. (some col.), digital ;24 cm.
Contained By:	Springer Nature eBook
Subject:	SolventsProperties.
Online resource:	https://doi.org/10.1007/978-3-031-31871-9
ISBN:	9783031318719$q(electronic bk.)

Solvent-induced interactions and forces in protein foldinghydrophobic-hydrophilic phenomena /
Ben-Naim, Arieh.

Solvent-induced interactions and forces in protein foldinghydrophobic-hydrophilic phenomena /[electronic resource] :by Arieh Ben-Naim. - Cham :Springer Nature Switzerland :2023. - xiii, 174 p. :ill. (some col.), digital ;24 cm. - Physical chemistry in action,2197-4357. - Physical chemistry in action..

Introduction, definitions and motivations for studying solvent-induced interactions -- A Brief Introduction to Statistical Thermodynamics -- Solvent-induced interactions and forces, definitions and connections with thermodynamics -- Hydrophobic interactions and forces -- Hydrophilic Interactions and Forces -- Implementation of the HϕI interactions and forces in some biochemical processes -- Appendix A. The BN3D model of water and the corresponding pair potential -- Appendix B. Solvation thermodynamics of water in liquid water.

This monograph presents the molecular theory and necessary tools for the study of solvent-induced interactions and forces. After introducing the reader to the basic definitions of solvent-induced interactions, the author provides a brief analysis of the statistical thermodynamics. The book thoroughly overviews the connection of those interactions with thermodynamics and consequently focuses on specifically discussing the hydrophobic-hydrophilic interactions and forces. The importance of the implementation of hydrophilic interactions and forces in various biochemical processes is thoroughly analyzed, while evidence based on theory, experiments, and simulated calculations supporting that hydrophilic interactions and forces are far more important than the corresponding hydrophobic effects in many biochemical processes such as protein folding, self-assembly of proteins, molecular recognitions, are described in detail. This title is of great interest to students and researchers working in the fields of chemistry, physics, biochemistry, and molecular biology.

ISBN: 9783031318719$q(electronic bk.)

Standard No.: 10.1007/978-3-031-31871-9doiSubjects--Topical Terms:

955782
Solvents
--Properties.

LC Class. No.: TP247.5

Dewey Class. No.: 541.3482

Solvent-induced interactions and forces in protein foldinghydrophobic-hydrophilic phenomena /
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505 0 $a Introduction, definitions and motivations for studying solvent-induced interactions -- A Brief Introduction to Statistical Thermodynamics -- Solvent-induced interactions and forces, definitions and connections with thermodynamics -- Hydrophobic interactions and forces -- Hydrophilic Interactions and Forces -- Implementation of the HϕI interactions and forces in some biochemical processes -- Appendix A. The BN3D model of water and the corresponding pair potential -- Appendix B. Solvation thermodynamics of water in liquid water.
520 $a This monograph presents the molecular theory and necessary tools for the study of solvent-induced interactions and forces. After introducing the reader to the basic definitions of solvent-induced interactions, the author provides a brief analysis of the statistical thermodynamics. The book thoroughly overviews the connection of those interactions with thermodynamics and consequently focuses on specifically discussing the hydrophobic-hydrophilic interactions and forces. The importance of the implementation of hydrophilic interactions and forces in various biochemical processes is thoroughly analyzed, while evidence based on theory, experiments, and simulated calculations supporting that hydrophilic interactions and forces are far more important than the corresponding hydrophobic effects in many biochemical processes such as protein folding, self-assembly of proteins, molecular recognitions, are described in detail. This title is of great interest to students and researchers working in the fields of chemistry, physics, biochemistry, and molecular biology.
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