1. Contributions to the catalytic efficiency of enzymes, and the binding of ligands to receptors, from improvements in packing within enzymes and receptors -- 2. Structural interpretation of pH and salt-dependent processes in proteins with computational methods -- 3. Electrostatic basis for bioenergetics -- 4. Local and global control mechanisms in allosteric threonine deaminase -- 5. Methods for analyzing cooperativity in phosphoglycerate dehydrogenase -- 6. Fluorescent probes applied to catalytic cooperativity in ATP synthase -- 7. Measurement of energetics of conformational change in cobalamin-dependent methionine synthase -- 8. Spectroscopic and kinetic methods for ligand-protein interactions of glutamate receptor -- 9. Quantitative analysis and interpretation of allosteric behavior -- 10. The immobilized template assay for measuring cooperativity in eukaryotic transcription complex assembly -- 11. Characterization of the cargo attachment complex of cytoplasmic dynein using NMR and mass spectrometry -- 12. Circular dichroism of protein-folding intermediates -- 13. Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of staphylococcus aureus aldolase -- 14. Kinetic and spectroscopic analysis of early events in protein folding -- 15. Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding -- 16. Cooperativity principles in protein folding -- 17. Native state hydrogen-exchange analysis of protein folding and protein motional domains -- 18. The preparations of ¹⁹F-labeled proteins for NMR studies.