Energetics of biological macromolecules. Part D / edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers.

Format:

Book

Contributor:

Holt, Jo M.

Johnson, Michael L., 1947-

Ackers, Gary K.

Series:

Methods in enzymology ; v. 379.

Methods in enzymology, 0076-6879 ; v. 379

Language:

English

Subjects (All):

Allosteric proteins.

Bioenergetics.

Cooperative binding (Biochemistry).

Macromolecules.

Thermodynamics.

Physical Description:

1 online resource (315 p.)

Place of Publication:

San Diego : Elsevier/Academic Press, c2004.

Language Note:

English

Summary:

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.*Methods for Evaluating Cooperativity in a Dimeric Hemoglobin*Multiple-Binding of Ligands to a Linear Biopolymer*Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions*Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural and Kinetic Analysis

Contents:

Front Cover; Energetics of Biological Macromolecules; Copyright Page; Table of Contents; Contributors to Volume 379; Preface; Volumes in Series; Section I: Cooperative Binding; Chapter 1. Analyzing Intermediate State Cooperativity in Hemoglobin; Chapter 2. Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity; Chapter 3. Evaluating Cooperativity in Dimeric Hemoglobins; Chapter 4. Measuring Assembly and Binding in Human Embryonic Hemoglobins; Chapter 5. Small-Angle Scattering Techniques for Analyzing Conformational Transitions in Hemocyanins

Chapter 6. Multivalent Protein-Carbohydrate Interactions: Isothermal Titration Microcalorimetry StudiesChapter 7. Calorimetric Analysis of Mutagenic Effects on Protein-Ligand Interactions; Chapter 8. Multiple Binding of Ligands to a Linear Biopolymer; Chapter 9. Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy; Chapter 10. Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions

Chapter 11. Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure-FunctionChapter 12. Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural, and Kinetic Analysis; Chapter 13. Distance Parameters Derived from Time- Resolved Fo ̈ rster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions; Author Index; Subject Index

Notes:

Description based upon print version of record.

Includes bibliographical references and indexes.

ISBN:

9786611011468

9781281011466

1281011460

9780080497174

0080497179

OCLC:

808616228