UID:
almafu_9960073127202883
Umfang:
1 online resource (485 p.)
ISBN:
1-281-71275-2
,
9786611712754
,
0-08-058224-9
Serie:
Advances in protein chemistry ; v. 51
Inhalt:
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
Anmerkung:
Description based upon print version of record.
,
Front Cover; Advances in Protein Chemistry, Volume 51; Copyright Page; Contents; Introduction; Chapter 1. Electrostatic Contributions to Molecular Free Energies in Solution; I. Introduction; II. Theory and Calculational Methods; III. Applications; IV. Outlook; References; Chapter 2. Site-Specific Analysis of Mutational Effects in Proteins; I. Introduction; II. The Reference Cycle; III. Structural Mapping of Energetics; IV. Site-Specific Analysis of Mutational Effects in Proteins; V. Site-Specific Dissection of Thrombin Specificity; VI. Concluding Remarks; References
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Chapter 3. Allosteric Transitions of the Acetylcholine ReceptorI. Introduction; II. Mechanistic Models; III. Recovery from Desensitization; IV. Kinetic Basis of Dose-Response Curves; V. Multiple Phenotypes; VI. Deductions from Single-Channel Measurements; VII. Allosteric Effectors and Coincidence Detection; VIII. General Considerations; References; Chapter 4. Deciphering the Molecular Code of Hemoglobin Allostery; I. Introduction; II. Overview; III. Binding Curves and Stoichiometric Information; IV. Site-Specific Aspects of Oxygen Binding
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V. Experimental Determination of Site-Specific Cooperativity TermsVI. How the Molecular Code Was Deciphered; VII. Concluding Remarks; References; Chapter 5. Statistical Thermodynamic Linkage between Conformational and Binding Equilibria; I. Introduction; II. The Most Probable Distribution; III. Coupling of Statistical Weights to Ligands; IV. Modulation of Distribution of States by Specific Ligands; V. Modulation of Distribution of States by Denaturants; VI. Ligand-Induced Conformational Changes; VII. The Distribution of Conformational States According to Their Gibbs Energy
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VIII. Is the Unfolded State the State with the Highest Gibbs Energy?IX. The Gibbs Energy Scale of Conformational States; X. Statistical Descriptors of the Conformational Ensemble; XI. Conclusions; References; Chapter 6. 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; I. Introduction; II. Overview of Concentration-Dependent Effects of Perturbing Solutes on Processes Involving Biopolymers
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III. Preferential Interaction Coefficients as Fundamental Measures of Thermodynamic Effects due to Solute-Biopolymer InteractionsIV. Preferential Interactions of Nonelectrolyte Molecules with an Uncharged Biopolymer; V. Preferential Interactions of Electrolyte Ions with a Charged Biopolymer; 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
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VII. Two-Domain Predictions of Functional Forms of Effects of Nonelectrolyte Concentration on Equilibria (Kobs) and Transition Temperatures ( Tm ) of Uncharged Biopolymers in Aqueous Solution
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English
Weitere Ausg.:
ISBN 0-12-034251-0
Sprache:
Englisch
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