1. Analyzing intermediate state cooperativity in hemoglobin -- 2. Nuclear magnetic resonance spectroscopy in the study of hemoglobin cooperativity -- 3. Evaluating cooperativity in dimeric hemoglobins -- 4. Measuring assembly and binding in human embryonic hemoglobins -- 5. Small-angle scattering techniques for analyzing conformational transitions in hemocyanins -- 6. Multivalent protein-carbohydrate interactions: isothermal titration microcalorimetry studies -- 7. Calorimetric analysis of mutagenic effects on protein-ligand interactions -- 8. Multiple binding of ligands to a linear biopolymer -- 9. Probing site-specific energetics in proteins and nucleic acids by hydrogen exchange and nuclear magnetic resonance spectroscopy -- 10. Fluorescence quenching methods to study protein-nucleic acid interactions -- 11. Thermodynamics, protein modification, and molecular dynamics in characterizing lactose repressor protein: strategies for complex analyses of protein structure-function -- 12. Linked equilibria in biotin repressor function: thermodynamic, structural and kinetic analysis -- 13. Distance parameters derived from time-resolved Forster resonance energy transfer measurements and their use in structural interpretations of thermodynamic quantities associated with protein-DNA interactions.