Energetics of Biological Macromolecules

✍ Scribed by Michael L. Johnson, Gary K. Ackers (Eds.)

• Publisher: Academic Press
• Year: 1995
• Tongue: English
• Leaves: 803
• Series: Methods in Enzymology 259
• Edition: 1
• Category: Library

✦ Synopsis

The critically acclaimed laboratory standard for forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerlyawaited, frequently consulted, and praised by researchers and reviewers alike. More than 250 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

Key Features
Thermodynamics as a tool for understanding molecular logic
Thermal denaturation methods in the study of protein folding
Predicting thermodynamic properties of RNA
Sedimentation equilibrium as a thermodynamic tool
Molecular volume
Thermodynamic parameters from hydrogen exchange measurements

✦ Table of Contents

Content:
Contributors to volume 259
Pages xi-xiii

Preface
Pages xv-xvi
Michael L. Johnson, Gary K. Ackers

Volumes in series
Pages xvii-xxxi

[1] Pathway of allosteric control as revealed by intermediate states of hemoglobin Original Research Article
Pages 1-19
Jo M. Holt, Gary K. Ackers

[2] Probes of energy transduction in enzyme catalysis Original Research Article
Pages 19-43
Yingwen Huang, D.W. Bolen

[3] Macromolecules and water: Probing with osmotic stress Original Research Article
Pages 43-94
V.Adrian Parsegian, R.Peter Rand, Donald C. Rau

[4] Linkage of protein assembly to protein-DNA binding Original Research Article
Pages 95-127
Isaac Wong, Timothy M. Lohman

[5] Linkage at steady state: Allosteric transitions of thrombin Original Research Article
Pages 127-144
Enrico Di Cera, Quoc D. Dang, Youhna Ayala, Alessandro Vindigni

[6] Thermal denaturation methods in the study of protein folding Original Research Article
Pages 144-168
Ernesto Freire

[7] Kinetics of lipid membrane phase transitions: A volume perturbation calorimeter study Original Research Article
Pages 169-182
Lubin Chen, Rodney L. Biltonen, Michael L. Johnson

[8] Tight binding affinities determined from thermodynamic linkage to protons by titration calorimetry Original Research Article
Pages 183-194
Michael L. Doyle, Godfrey Louie, Paul R. Dal Monte, Theodore D. Sokoloski

[9] Calorimetric methods for interpreting protein—Ligand interactions Original Research Article
Pages 194-221
Harvey F. Fisher, Narinder Singh

[10] Extracting thermodynamic data from equilibrium melting curves for oligonucleotide order-disorder transitions Original Research Article
Pages 221-242
Kenneth J. Breslauer

[11] Predicting thermodynamic properties of RNA Original Research Article
Pages 242-261
Martin J. Serra, Douglas H. Turner

[12] Thermodynamics and mutations in RNA—Protein interactions Original Research Article
Pages 261-281
Kathleen B. Hall, James K. Kranz

[13] Melting studies of RNA unfolding and RNA—Ligand interactions Original Research Article
Pages 281-305
David E. Draper, Thomas C. Gluick

[14] Structural-perturbation approaches to thermodynamics of site-specific protein—DNA interactions Original Research Article
Pages 305-344
Linda Jen-Jacobson

[15] Thermodynamic parameters from hydrogen exchange measurements Original Research Article
Pages 344-356
Yawen Bai, Joan J. Englander, Leland Mayne, John S. Milne, S.Walter Englander

[16] Application of pressure to biochemical equilibria: The other thermodynamic variable Original Research Article
Pages 357-377
Catherine A. Royer

[17] Molecular volume Original Research Article
Pages 377-395
Lorraine M. Rellick, Wayne J. Becktel

[18] Hydrostatic and osmotic pressure as tools to study macromolecular recognition Original Research Article
Pages 395-427
Clifford R. Robinson, Stephen G. Sligar

[19] Sedimentation equilibrium as thermodynamic tool Original Research Article
Pages 427-452
Thomas M. Laue

[20] Footprint phenotypes: Structural models of DNA-binding proteins from chemical modification analysis of DNA Original Research Article
Pages 452-468
Jie Yang, Jannette Carey

[21] Low-temperature electrophoresis methods Original Research Article
Pages 468-487
Michele Perrella, Ilya Denisov

[22] Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins Original Research Article
Pages 487-512
Maurice R. Eftink

[23] Probing structural and physical basis of protein energetics linked to protons and salt Original Research Article
Pages 512-538
E. Bertrand GarcГ­a-Moreno

[24] Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding Original Research Article
Pages 538-554
C.N. Pace

[25] Analyzing solvent reorganization and hydrophobicity Original Research Article
Pages 555-576
B. Lee

[26] Simple force field for study of peptide and protein conformational properties Original Research Article
Pages 576-589
Trevor P. Creamer, George D. Rose

[27] Probes for analysis of stability of different variants of aspartate aminotransferase Original Research Article
Pages 590-608
Marino Martinez-Carrion, Antonio Artigues, Alan Berezov, Maria L. Bianconi, Alejandro M. Reyes, Ana Iriarte

[28] Thermodynamic approaches to understanding aspartate transcarbamylase Original Research Article
Pages 608-628
Norma M. Allewell, Vince J. Licata

[29] On the interpretation of data from isothermal processes Original Research Article
Pages 628-720
Rufus Lumry

Author index
Pages 721-744

Subject index
Pages 745-761