Overview

This book starts out by presenting the evidence for the importance of hydrophilic interactions in biochemical processes and then goes on to describe the applications of the hydrophilic interactions in these processes, specifically protein folding, protein association, self assembly and molecular recognition.In this volume it is shown that the new paradigm, based on the hydrophilic effect, brings us as close as one can hope to the solutions of the protein folding problem, as well as the problem of self assembly and molecular recognition. In addition, the new paradigm also provides an explanation of the high solubility of globular proteins.The change in the paradigm is shown symbolically in the cover design of this book.

Full Product Details

Author:   Arieh Ben-naim (The Hebrew Univ Of Jerusalem, Israel)
Publisher:   World Scientific Publishing Co Pte Ltd
Imprint:   World Scientific Publishing Co Pte Ltd
Dimensions:   Width: 15.50cm , Height: 4.30cm , Length: 22.90cm
Weight:   1.633kg
ISBN:  

9789814383127

ISBN 10:   9814383120
Pages:   480
Publication Date:   22 June 2011
Audience:   College/higher education ,  Professional and scholarly ,  Tertiary & Higher Education ,  Professional & Vocational
Format:   Paperback
Publisher's Status:   Active
Availability:   Out of stock  
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Table of Contents

"Introduction, the Main Problem and the Main Tools: The General Problem; Forces and Driving Forces; Definition of the Solvation Process and the Corresponding Thermodynamic Quantities; The Conditional Solvation Process; Some Numerical Values of Solvation Thermodynamics; Hydrophobicity Scales; Some Numerical Values of the Pairwise Hydrophobic and Hydrophilic Interactions; Dissection of the Solvation Gibbs Energy of a Globular Protein; Dissection of the Solvation Gibbs Energy of a Denatured Protein; The Relationship between the Standard Gibbs Energy of a Reaction and Solvation Gibbs Energies; The Various Solvent-Induced Contributions to the Driving Force for Protein Folding; Concluding Remarks and Some Suggestions for the Future; Solvation and Solubility of Globular Proteins: Definition of Solubility and its Relationship to the Solvation Gibbs Energy; Solvation Gibbs Energy of a Model Globular Protein; Estimation of the Solvation Gibbs Energy of Real Proteins; The Relation between Solubility and Solvation Gibbs Energy for Moderately Soluble Proteins; A Possible Explanation for an Apparently Paradoxical Experimental Finding; The Effect of the Addition of a Solute on the Solvation Gibbs Energy; Concluding Remarks and Suggestions for Future Research; Protein Folding: The Chemical Equilibrium; Definition of the Folded and Unfolded Forms; Formal Dissection of the Solvent-Induced Effect on Protein Folding into ""Small"" Ingredients; Methods of Studying and Estimating the Various Contributions to δG; Summary of the Factors Involved in the Stability of the Native Protein; The Problem of the Preferential Protein Folding Pathways of Proteins; Energy Landscapes, Gibbs Energy Landscapes and Forces in Protein Folding; What Kind of Forces are Exerted on the Protein in the Process of Protein Folding?; The Forces in Action; Is there a ""Folding Code""?; Concluding Remarks and Suggestions for Future Research; Association and Self-Assembly of Biomolecules: Thermodynamics and Statistical Thermodynamics of the Association Process; The Factors Involved in the Association of Two Biomolecules; Association of Two Hypothetical Globular Proteins; HϕO or HϕI Interaction: Which is More Important in the Association Process?; Association by the Complete Absorption of a Small Solute into a Big Solute; Specificity of the Binding Mode; Molecular Recognition; Self-Assembly of Macromolecules; Strong Solvent-Induced Forces between Macromolecules; Concluding Remarks and Suggestions for Future Research."

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