Energetics of biological macromolecules

Author(s)

• Johnson, Michael L.
• Ackers, Gary K.
• Holt, Jo M.

Bibliographic Information

Energetics of biological macromolecules

edited by Michael L. Johnson, Gary K. Ackers

（Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 259, 295, 323, 379-380）

Academic Press, c1995-

• [pt. A]
• pt. B
• pt. C
• pt. D
• pt. E

Note

Pts. D-E: edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers

Pts. D-E: publisher changed to Elsevier Academic Press

Includes bibliographical references and indexes

Description and Table of Contents

Volume

[pt. A] ISBN 9780121821609

Description

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.

Table of Contents

J.M. Holt and G.K. Ackers, Pathway of Allosteric Control as Revealed by Intermediate States of Hemoglobin. Y. Huang and D.W. Bolen, Probes of Energy Transduction in Enzyme Catalysis. V.A. Parsegian, R.P. Rand, and D.C. Rau, Macromolecules and Water: Probing with Osmotic Stress. I. Wong and T.M. Lohman, Linkage of Protein Assembly to Protein-DNA Binding. E. Di Cera, Q.D. Dang, Y. Ayala, and A. Vindigni, Linkage at Steady State: Allosteric Transitions of Thrombin. E. Freire, Thermal Denaturation Methods in Study of Protein Folding. L. Chen, R.L. Biltonen, and M.L. Johnson, Kinetics of Lipid Membrane Phase Transitions: A Volume Perturbation Calorimeter Study. M.L. Doyle, G. Louie, P. Dal Monte, and T. Sokoloski, Tight Binding Affinities Determined from the Thermodynamic Linkage to Protons by Titration Calorimetry. H.F. Fisher and N. Singh, Calorimetric Methods for Interpreting Protein-Ligand Interactions. K.J. Breslauer, Extracting Thermodynamic Data from Equilibrium Melting Curves for Oligonucleotide Order-Disorder Transitions. M.J. Serra and D.H. Turner, Predicting Thermodynamic Properties of RNA. K.B. Hall and J.K. Kranz, Thermodynamics and Mutations in RNA-Protein Interactions. D.E. Draper and T.C. Gluick, Melting Studies of RNA Unfolding and RNA-Ligand Interactions. L. Jen-Jacobson, Structural-Perturbation Approaches to Thermodynamics of Site-Specific Protein-DNAInteractions. Y. Bai, J.J. Englander, L. Mayne, J.S. Milne, and S.W. Englander, Thermodynamic Parameters from Hydrogen Exchange Measurements. C.A. Royer, Application of Pressure to Biochemical Equilibria: The Other Thermodynamic Variable. L.M. Rellick and W.J. Becktel, Molecular Volume. C.R. Robinson and S.G. Sligar, Hydrostatic and Osmotic Pressure as Tools to Study Macromolecular Recognition. T.M. Laue, Sedimentation Equilibrium as Thermodynamic Tool. J. Yang and J. Carey, Footprint Phenotypes: Structural Models of DNA-Binding Proteins from Chemical Modification Analysis of DNA. M. Perrella and I. Denisov, Low-Temperature Electrophoresis Methods. M.R. Eftink, Use of Multiple Spectroscopic Methods to Monitor Equilibrium Unfolding of Proteins. B. Garcia-Moreno, Probing Structural and Physical Basis of Protein Energetics Linked to Protons and Salt. C.N. Pace, Evaluating Contribution of Hydrogen Bonding and Hydrophobic Bonding to Protein Folding. B. Lee, Analyzing Solvent Reorganization and Hydrophobicity. T.P. Creamer and G.D. Rose, Simple Force Field for Study of Peptide and Protein Conformational Properties. M. Martinez-Carrion, A. Artigues, A. Berezov, M.L. Bianconi, A.M. Reyes, and A. Iriarte, Probes for Analysis of Stability of Different Variants of Aspartate Aminotransferase. N.M. Allewell and V.J. LiCata, Thermodynamic Approaches to Understanding Aspartate Transcarbamylase. R. Lumry, On the Interpretation of Data from Isothermal Processes. Author Index. Subject Index.

Volume

pt. B ISBN 9780121821968

Description

General Description of the Volume: The very existence of biological structures and their functional interactions are dictated by energetic relationships. Thus the central theme of this volume is that thermodynamic methods, i.e. techniques that probe the energetics of biological macromolecules, now comprise a powerful and practical family of tools for research in modern biology. The application of thermodynamics and statistical thermodynamics to biochemical and biophysical systems is presented. This volume supplements Methods in Enzymology, Volume 259. General Description of the Series: The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.

Table of Contents

C.A. Rohl and R.L. Baldwin, Deciphering Rules of Helix Stability in Peptides. N.R. Kallenbach and E.J. Spek, Modified Amino Acids as Probes of Helix Stability. V.J. LiCata and N.M. Allewell, Measuring Hydration Changes of Proteins in Solution: Applications of Osmotic Stress and Structure-Based Calculations. S.H. White, W.C. Wimley, A.S. Ladokhin, and K. Hristova, Protein Folding in Membranes: Determining Energetics of Peptide-Bilayer Interactions. M.L. Doyle and P. Hensley, Tight Ligand Binding Affinities Determined from Thermodynamic Linkage to Temperature by Titration Calorimetry. I. Luque and E. Freire, Structure-Based Prediction of Binding Affinities and Molecular Design of Peptide Ligands. A.P. Minton, Molecular Crowding: Analysis of Effects of High Concentrations of Inert Cosolutes on Biochemical Equilibria and Rates in Terms of Volume Exclusion. J.M. Schwehm and W.E. Stites, Application of Automated Methods for Determination of Protein Conformational Stability. P. Beroza and D.A. Case, Calculations of Proton Binding Thermodynamics in Proteins. A.L. Klinger and G.K. Ackers, Analysis of Spectra from Multiwavelength Oxygen Binding Studies of Mixed Metal Hybrid Hemoglobins. L. Benazzi, R. Russo, M. Ripamonti, and M. Perrella, Study of the Bohr Effect in Hemoglobin Intermediates. P.W. Chun, Application of Planck-Benzinger Relationships to Biology. T.A. Morton and D.G. Myszka, Kinetic Analysis of Macromolecular Interactions Using Surface Plasmon Resonance Biosensors. B.M. Baker and K.P. Murphy, Prediction of Binding Energetics from Structure Using Empirical Parameterization. M.A. McLean, C. Di Primo, E. Deprez, G. Hui Bon-Hoa, and S.G. Sligar, Photoacoustic Calorimetry of Proteins. H.F. Fisher and J. Tally, Isoergonic Cooperativity: A Novel Form of Allostery. L. Indyk and H.F. Fisher, Theoretical Aspects of Isothermal Titration Calorimetry. V.A. Bloomfield and I. Rouzina, Use of Poisson-Boltzmann Equation to Analyze Ion Binding to DNA. B. Sclavi, S. Woodson, M. Sullivan, M. Chance, and M. Brenowitz, Following the Folding of RNA with Time-Resolved Synchrotron X-Ray Footprinting. D.F. Senear, L.T. Perini, and S.A. Gavigan, Analysis of Interactions Between CytR and CRP at CytR-Regulated Promoters. D. Beckett, Energetic Methods to Study Bifunctional Biotin Operon Repressor. E.K. Merabet, D.S. Burz, and G.K. Ackers, Thermal Melting Properties of C-Terminal Domain Mutants of Bacteriophage l cI Repressor. J.T. Mason, Investigation of Phase Transitions in Bilayer Membranes. T.M. Laue, H.K. Shepard, T.M. Ridgeway, T.P. Moody, and T.J. Wilson, Membrane-Confined Analytical Electrophoresis. Author Index. Subject Index.

Volume

pt. C ISBN 9780121822248

Description

Volume 323 of Methods in Enzymology is dedicated to the energetics of biological macromolecules. Understanding the molecular mechanisms underlying a biological process requires detailed knowledge of the structural relationships within the system and an equally detailed understanding of the energetic driving forces that control the structural interactions. This volume presents modern thermodynamic techniques currently being utilized to study the energetic driving forces in biological systems. It will be a useful reference source and textbook for scientists and students whose goal is to understand the energetic relationships between macromoleculer structures and biological functions. This volume supplements Volumes 259 and Volume 295 of Methods in Enzymology.

Volume

pt. D ISBN 9780121827830

Description

This volume focuses on the cooperative binding aspects of energetics in biological macromolecules. Methodologies such as NMR, small-angle scattering techniques for analysis, calorimetric analysis, fluorescence quenching, and time resolved FRET measurements are discussed.

Table of Contents

• Analyzing Intermediate State Cooperativity in Hemoglobin
• Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity
• Evaluating Cooperativity in Dimeric Hemoglobins
• Measuing Assembly and Binding in Human Embryonic Hemoglobins
• Small-Angle Scattering Techniques for Analyzing
• Conformational Transitions in Hemocyanins
• Multivalent Protein-Carbohydrate Interactions: Isothermal Titration Microcalorimetry Studies
• Calorimetric Analysis of Mutagenic Effects on Protein-Ligand Interactions
• Multiple Binding of Ligands to a Linear Biopolymer
• Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy
• Fluorescence Quenching Methods to Study Protein-Nucleic Acid interactions
• Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure-Function
• Linked Equilibria in Biotin Repressor Function: Thermodynamics, Structural, and Kinetic Analysis
• Distance Parameters Derived from Time-Resolved Foerster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions

Volume

pt. E ISBN 9780121827847

Description

Energetics of Biological Macromolecules, Part E focuses on methods related to allosteric enzymes and receptors, including fluorescent proves, spectroscopic methods and quantitative analysis as well as on cooperativity in protein folding. NMR and mass spectrometry methods are discussed.

by "Nielsen BookData"

Details

• NCID: BA26042225
• ISBN:
  • 0121821609
  • 012182196X
  • 0121822249
  • 0121827836
  • 0121827844
• Country Code: us
• Title Language Code: eng
• Text Language Code: eng
• Place of Publication: San Diego, Calif. ; Tokyo
• Pages/Volumes: v.
• Size: 24 cm
• Classification:
  • NLM : W1
• Subject Headings:
  • MESH : Allosteric Regulation
  • MESH : Energy Metabolism
  • MESH : Macromolecular Systems
  • MESH : Molecular Conformation
  • MESH : Thermodynamics
• Parent Bibliography ID:
  • BA00197543