Energetics of Biological Macromolecules, Part E
Published on 14. May 2014
478 pages
978-0-08-049718-1 (ISBN)
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.
- Allosteric Enzymes and Receptors
- Cooperativity in Protein Folding and Assembly
More details
Series
Edition
New ed.
Language
English
Place of publication
San Diego
United States
Product notice
Windows
Illustrations
Approx. 200 illustrations
ISBN-13
978-0-08-049718-1 (9780080497181)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Other editions
Additional editions
Jo M. Holt | Michael L. Johnson | Gary K. Ackers
Energetics of Biological Macromolecules, Part E: Volume 380
Book
04/2004
Academic Press
€167.41
Shipment within 15-20 days
Persons
Content
- Cover
- Table of Contents
- Contributors to Volume 380
- Preface
- Volumes in Series
- Section I: Allosteric Enzymes and Receptors
- Chapter 1. Contributions to the Catalytic Efficiency of Enzymes, and the Binding of Ligands to Receptors, from Improvements in Packing within Enzymes and Receptors
- Chapter 2. Structural Interpretation of pH and Salt-Dependent Processes in Proteins with Computational Methods
- Chapter 3. Electrostatic Basis for Bioenergetics
- Chapter 4. Local and Global Control Mechanisms in Allosteric Threonine Deaminase
- Chapter 5. Methods for Analyzing Cooperativity in Phosphoglycerate Dehydrogenase
- Chapter 6. Fluorescent Probes Applied to Catalytic Cooperativity in ATP Synthase
- Chapter 7. Measurement of Energetics of Conformational Change in Cobalamin-Dependent Methionine Synthase
- Chapter 8. Spectroscopic and Kinetic Methods for Ligand-Protein Interactions of Glutamate Receptor
- Chapter 9. Quantitative Analysis and Interpretation of Allosteric Behavior
- Section II: Cooperativity in Protein Folding and Assembly
- Chapter 10. The Immobilized Template Assay for Measuring Cooperativity in Eukaryotic Transcription Complex Assembly
- Chapter 11. Characterization of the Cargo Attachment Complex of Cytoplasmic Dynein Using NMR and Mass Spectrometry
- Chapter 12. Circular Dichroism of Protein-Folding Intermediates
- Chapter 13. Amide Hydrogen Exchange/Mass Spectrometry Applied to Cooperative Protein Folding: Equilibrium Unfolding of Staphylococcus aureus Aldolase
- Chapter 14. Kinetic and Spectroscopic Analysis of Early Events in Protein Folding
- Chapter 15. Hydrogen-Exchange Strategies Applied to Energetics of Intermediate Processes in Protein Folding
- Chapter 16. Cooperativity Principles in Protein Folding
- Chapter 17. Native State Hydrogen-Exchange Analysis of Protein Folding and Protein Motional Domains
- Chapter 18. The Preparation of 19F-Labeled Proteins for NMR Studies
- Author Index
- Subject Index
