Quotations |
List of Abbreviations |
Preface |
Acknowledgements |
Introduction, the Main Problem and the Main Tools / 1: |
The General Problem / l.l: |
Forces and Driving Forces / 1.2: |
Definition of the Solvation Process and the Corresponding Thermodynamic Quantities / 1.3: |
The Conditional Solvation Process / 1.4: |
Some Numerical Values of Solvation Thermodynamics / 1.5: |
Solvation of hydrophilic molecules or groups / 1.5.1: |
Solvation of hydrophobic molecules or groups / 1.5.2: |
Hydrophobicity Scales / 1.6: |
Some Numerical Values of the Pairwise Hydrophobic and Hydrophilic Interactions / 1.7: |
Pairwise hydrophobic{H?0)interaction / 1.7.1: |
Pairwise hydrophilic (H?I)interaction / 1.7.2: |
Potential of average force for pairs of side chains of amino acids / 1.7.3: |
Dissection of the Solvation Gibbs Energy of a Globular Protein / 1.8: |
Dissection of the Solvation Gibbs Energy of a Denatured Protein / 1.9: |
The Relationship between the Standard Gibbs Energy of a Reaction and Solvation Gibbs Energies / 1.10: |
The Various Solvent-Induced Contributions to the Driving Force for Protein Folding / 1.11: |
The solvation of the hard part / 1.11.1: |
The solvation of the soft part / 1.11.2: |
The contribution of the functional groups (FGs) exposed to the solvent / 1.11.3: |
Concluding Remarks and Some Suggestions for the Future / 1.12: |
Solvation and Solubility of Globular Proteins / 2: |
Definition of Solubility and its Relationship to the Solvation Gibbs Energy / 2.1: |
Solvation Gibbs Energy of a Model Globular Protein / 2.2: |
Estimation of the Solvation Gibbs Energy of Real Proteins / 2.3: |
The Relation between Solubility and Solvation Gibbs Energy for Moderately Soluble Proteins / 2.4: |
A Possible Explanation for an Apparently Paradoxical Experimental Finding / 2.5: |
The Effect of the Addition of a Solute on the Solvation Gibbs Energy / 2.6: |
Concluding Remarks and Suggestions for Future Research / 2.7: |
Protein Folding / 3: |
The Chemical Equilibrium / 3.1: |
Definition of the Folded and Unfolded Forms / 3.2: |
Formal Dissection of the Solvent-Induced Effect on Protein Folding into "Small" Ingredients / 3.3: |
Methods of Studying and Estimating the Various Contributions to $G / 3.4: |
Summary of the Factors Involved in the Stability of the Native Protein / 3.5: |
The Problem of the Preferential Protein Folding Pathways of Proteins / 3.6: |
Energy Landscapes, Gibbs Energy Landscapes and Forces in Protein Folding / 3.7: |
What Kind of Forces are Exerted on the Protein in the Process of Protein Folding? / 3.8: |
The Forces in Action / 3.9: |
Is there a "Folding Code"? / 3.10: |
Association and Self-Assembly of Biomolecules / 3.11: |
Thermodynamics and Statistical Thermodynamics of the Association Process / 4.1: |
The Factors Involved in the Association of two Biomolecules / 4.2: |
Association of two Hypothetical Globular Proteins / 4.3: |
The "driving force" for dimerization / 4.3.1: |
Virtual dimers, probabilistic considerations / 4.3.2: |
Some numerical estimates of various contributions to the total PMF / 4.3.3: |
H?0 or, H?I Interaction: Which is More Important in the Association Process? / 4.4: |
Association of P and L in an ideal gas phase / 4.4.1: |
Association in an organic liquid / 4.4.2: |
Association in aqueous solutions / 4.4.3: |
Enhancement of the H?O Mode by Strengthening the H?I Effects / 4.4.4: |
Association by the Complete Absorption of a Small Solute into a Big Solute / 4.5: |
Absorption without conformational changes in P / 4.5.1: |
Absorption with conformational changes in P / 4.5.2: |
Specificity of the Binding Mode; Molecular Recognition / 4.6: |
The lock-and-key model for molecular recognition / 4.6.1: |
Molecular recognition through the solvant / 4.6.2: |
Self-Assembly of Macromolecules / 4.7: |
Strong Solvent-Induced Forces between Macromolecules / 4.8: |
Solvent-induced force by means of one-water bridges / 4.8.1: |
Solvent-Induced Force by Means of Two-Water Bridges / 4.8.2: |
Stronger forces between H?I surfaces / 4.8.3: |
The General Statistical Mechanical Expression for the Chemical Potential and the Pseudo-Chemical Potential / 4.9: |
The Pseudo-Chemical Potential and the Solvation Helmholtz Energy of a Molecule Having Internal Rotational Degrees of Freedom / Appendix B: |
The Potential of Mean Force (PMF) and the Solvent-Induced Force / Appendix C: |
Conditional Solvation and Conditional Correlation / Appendix D: |
Non-Additivity of the Potential of Mean Force and of the Solvation Gibbs Energy / Appendix E: |
The Statistical Mechanical Definition of Independence of Solvation and of Conditional Solvation / Appendix F: |
Approximate Estimates of the H?I Interaction between Two, Three and Four H?I Groups at a Distance of 4.5 A / Appendix G: |
Evaluating The Inadequacy of Kauzmann's Model for the Role of the H?O Effect in Protein Folding / Appendix H: |
The Cracks in the Hydrogen Bond Inventory Argument / Appendix I: |
Can "Statistical Potential," Derived from Protein Structures, be Interpreted as a Potential of Mean Force? / Appendix J: |
Work of Creating a Cavity and the Probability of Finding a Cavity in a Solvent / Appendix K: |
H?I Interactions and Solubility of Isomeric Compounds / Appendix L: |
Further Inflating the Already Inflated Value of the H?0 Effect / Appendix M: |
The Anfinsen Dogma and the "Thermodynamic Hypothesis" Applied to the Process of Protein Folding / Appendix N: |
Entropy-Enthalpy Compensation; from an Exact Theorem to an Approximate Manifestation / Appendix O: |
Probability of Finding a Specific Configuration of a Protein and the Work Required to Obtain that Configuration / Appendix P: |
The Many Faces of Reversibility and Irreversibility / Appendix Q: |
Cooperativity in Protein Folding? / Appendix R: |
Local Densities of Water Molecules near H?I Groups / Appendix S: |
What Drives the "Driving Force?" / Appendix T: |
References |
Index |
Quotations |
List of Abbreviations |
Preface |
Acknowledgements |
Introduction, the Main Problem and the Main Tools / 1: |
The General Problem / l.l: |