Energetics of Biological Macromolecules, Part E

1. Auflage 2004
ISBN: 978-0-08-049718-1
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 443 Seiten, Web PDF

This volume 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

Autoren/Hrsg.

Inhaltsverzeichnis

1;Cover;1
2;Table of Contents;8
3;Contributors to Volume 380;10
4;Preface;12
5;Volumes in Series;14
6;Section I: Allosteric Enzymes and Receptors;36
6.1;Chapter 1. Contributions to the Catalytic Efficiency of Enzymes, and the Binding of Ligands to Receptors, from Improvements in Packing within Enzymes and Receptors;38
6.2;Chapter 2. Structural Interpretation of pH and Salt-Dependent Processes in Proteins with Computational Methods;55
6.3;Chapter 3. Electrostatic Basis for Bioenergetics;87
6.4;Chapter 4. Local and Global Control Mechanisms in Allosteric Threonine Deaminase;120
6.5;Chapter 5. Methods for Analyzing Cooperativity in Phosphoglycerate Dehydrogenase;141
6.6;Chapter 6. Fluorescent Probes Applied to Catalytic Cooperativity in ATP Synthase;167
6.7;Chapter 7. Measurement of Energetics of Conformational Change in Cobalamin-Dependent Methionine Synthase;187
6.8;Chapter 8. Spectroscopic and Kinetic Methods for Ligand–Protein Interactions of Glutamate Receptor;205
6.9;Chapter 9. Quantitative Analysis and Interpretation of Allosteric Behavior;222
7;Section II: Cooperativity in Protein Folding and Assembly;240
7.1;Chapter 10. The Immobilized Template Assay for Measuring Cooperativity in Eukaryotic Transcription Complex Assembly;242
7.2;Chapter 11. Characterization of the Cargo Attachment Complex of Cytoplasmic Dynein Using NMR and Mass Spectrometry;254
7.3;Chapter 12. Circular Dichroism of Protein-Folding Intermediates;277
7.4;Chapter 13. Amide Hydrogen Exchange/Mass Spectrometry Applied to Cooperative Protein Folding: Equilibrium Unfolding of Staphylococcus aureus Aldolase;320
7.5;Chapter 14. Kinetic and Spectroscopic Analysis of Early Events in Protein Folding;343
7.6;Chapter 15. Hydrogen-Exchange Strategies Applied to Energetics of Intermediate Processes in Protein Folding;363
7.7;Chapter 16. Cooperativity Principles in Protein Folding;385
7.8;Chapter 17. Native State Hydrogen-Exchange Analysis of Protein Folding and Protein Motional Domains;414
7.9;Chapter 18. The Preparation of 19F-Labeled Proteins for NMR Studies;435
8;Author Index;452
9;Subject Index;470