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Linkage Thermodynamics of Macromolecular Interactions,9780120342518
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Linkage Thermodynamics of Macromolecular Interactions

by ; ; ;
Edition:
1st
ISBN13:

9780120342518

ISBN10:
0120342510
Format:
Hardcover
Pub. Date:
5/20/1998
Publisher(s):
Elsevier Science
List Price: $180.00

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This is the 1st edition with a publication date of 5/20/1998.
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Summary

This volume commemorates the 50th anniversary of the appearance in Volume 4 in 1948 of Dr. Jeffries Wyman's famous paper in which he "laid down" the foundations of linkage thermodynamics. Experts in this area contribute articles on the state-of-the-art of this important field and on new developments of the original theory. Among the topics covered in this volume are electrostatic contributions to molecular free energies in solution; site-specific analysis of mutational effects in proteins; allosteric transitions of the acetylcholine receptor; and deciphering the molecular code of hemoglobin allostery.

Table of Contents

INTRODUCTION ix
Electrostatic Contributions to Molecular Free Energies in Solution
1(58)
MICHAEL SCHAEFER
HERMAN W. T. VAN VLIJMEN
MARTIN KARPLUS
I. Introduction
1(2)
II. Theory and Calculational Methods
3(17)
III. Applications
20(33)
IV. Outlook
53(1)
References
54(5)
Site-Specific Analysis of Mutational Effects in Proteins
59(62)
ENRICO DI CERA
I. Introduction
59(2)
II. The Reference Cycle
61(2)
III. Structural Mapping of Energetics
63(10)
IV. Site-Specific Analysis of Mutational Effects in Proteins
73(6)
V. Site-Specific Dissection of Thrombin Specificity
79(34)
VI. Concluding Remarks
113(2)
References
115(6)
Allosteric Transitions of the Acetylcholine Receptor
121(64)
STUART J. EDELSTEIN
JEAN-PIERRE CHANGEUX
I. Introduction
121(6)
II. Mechanistic Models
127(6)
III. Recovery from Desensitization
133(4)
IV. Kinetic Basis of Dose-Response Curves
137(4)
V. Multiple Phenotypes
141(8)
VI. Deductions from Single-Channel Measurements
149(14)
VII. Allosteric Effectors and Coincidence Detection
163(3)
VIII. General Considerations
166(7)
References
173(12)
Deciphering the Molecular Code of Hemoglobin Allostery
185(70)
GARY K. ACKERS
I. Introduction
185(5)
II. Overview
190(8)
III. Binding Curves and Stoichiometric Information
198(8)
IV. Site-Specific Aspects of Oxygen Binding
206(5)
V. Experimental Determination of Site-Specific Cooperativity Terms
211(10)
VI. How the Molecular Code Was Deciphered
221(25)
VII. Concluding Remarks
246(2)
References
248(7)
Statistical Thermodynamic Linkage between Conformational and Binding Equilibria
255(27)
ERNESTO FREIRE
I. Introduction
255(2)
II. The Most Probable Distribution
257(1)
III. Coupling of Statistical Weights to Ligands
257(2)
IV. Modulation of Distribution of States by Specific Ligands
259(3)
V. Modulation of Distribution of States by Denaturants
262(1)
VI. Ligand-Induced Conformational Changes
263(1)
VII. The Distribution of Conformational States According to Their Gibbs Energy
263(4)
VIII. Is the Unfolded State the State with the Highest Gibbs Energy?
267(2)
IX. The Gibbs Energy Scale of Conformational States
269(2)
X. Statistical Descriptors of the Conformational Ensemble
271(7)
XI. Conclusions
278(1)
References
278(4)
Analysis of Effects of Salts and Uncharged Solutes on Protein and Nucleic Acid Equilibria and Processes: A Practical Guide to Recognizing and Interpreting Polyelectrolyte Effects, Hofmeister Effects, and Osmotic Effects of Salts
282(74)
M. THOMAS RECORD, JR.
WENTAO ZHANG
CHARLES F. ANDERSON
I. Introduction
282(4)
II. Overview of Concentration-Dependent Effects of Perturbing Solutes on Processes Involving Biopolymers
286(9)
III. Preferential Interaction Coefficients as Fundamental Measures of Thermodynamic Effects due to Solute-Biopolymer Interactions
295(8)
IV. Preferential Interactions of Nonelectrolyte Molecules with an Uncharged Biopolymer
303(8)
V. Preferential Interactions of Electrolyte Ions with a Charged Biopolymer
311(8)
VI. Use of Three-Component Preferential Interaction Coefficients to Analyze Effects of Solute Concentration on Equilibrium Constants, Transition Temperatures, or Free Energy Changes of Biopolymer Processes
319(7)
VII. Two-Domain Predictions of Functional Forms of Effects of Nonelectrolyte Concentration on Equilibria (K(obs)) and Transition Temperatures (T(m)) of Uncharged Biopolymers in Aqueous Solution
326(4)
VIII. Polyelectrolyte and Two-Domain Predictions of Functional Forms of Effects of Salt Concentration on Equilibria (K(obs)) and Transition Temperatures (T(m)) of Charged Biopolymers in Aqueous Solution
330(19)
IX. Conclusions and Future Directions
349(1)
References
350(6)
Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated
356(77)
SERGE N. TIMASHEFF
I. Introduction
356(4)
II. Preferential Interactions
360(17)
III. Wyman Linkages in Preferential Interactions
377(10)
IV. Linkage Control of Protein Stability
387(22)
V. Linkage Control of Protein Reactions
409(7)
VI. Sources of Exclusion
416(7)
VII. Osmolytes
423(2)
VIII. Conclusion
425(3)
References
428(5)
AUTHOR INDEX 433(20)
SUBJECT INDEX 453


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