Energetics of biological macromolecules. Pt. E / edited by Jo M. Holt ... [et al.]. -- (Methods in Enzymology ; v. 380). -- Elsevier, 2004. -- (58.17435/C719/v.380/pt. E)

Contents:

1. Contributions to the Catalytic Efficiency of Enzymes, and the Binding of Ligands to Receptors, from Improvements in Packing within Enzymes and Receptors  3

2. Structural Interpretation of pH and Salt-Dependent Processes in Proteins with Computational Methods  20

3. Electrostatic Basis for Bioenergetics  52

4. Local and Blobal Control Mechanisms in Allosteric Threonine Deaminase  85

5. Methods for analyzing Cooperativity in Phosphoglycerate Dehydrogenase  106

6. Fluorescent Probes Applied to Catalytic Cooperativity in ATP Synthase  132

7. Measurement of Energetics of Conformational Change in Cobalamin-Dependent Methionine Synthase  152

8. Spectroscopic and Kinetic Methods for Ligand-Protein Interactions of Glutamate Receptor  170

9. Quantitative Analysis and Interpretation of Allosteric Behavior  187

10. The Immobilized Template Assay for Measuring Cooperativity in Eukaryotic Transcription Complex Assembly  207

11. characterization of the Cargo Attachment Complex of Cytoplasmic Dynein Using NMR and Mass Spectrometry  219

12. Circular Dichroism of Protein-folding Internediates  242

13. Amide Hydrogen Exchande/Mass Spectrometry Applied to Cooperative Protein Folding: Equilibrium Unfolding of Staphylococcus aureus Aldolase  285

14. Kinetic and Spectroscopic Analysis of Early Events in Protein Folding  308

15. Hydrogen-Exchange Strategies Applied to Energetics of Intermediate Processes in Protein Folding  328

16. Cooperativity Principles in Protein Folding  350

17. Native State Hydrogen-Exchange Analysis of Protein Folding and Protein Motional Domains  379

18. The Preparation of 19F-Labeled Proteins for NMR Studies  400