This volume focuses on the cooperative binding aspects of energetics in biological macromolecules. Methodologies such as NMR, small-angle scattering techniques for analysis, calorimetric analysis, fluorescence quenching, and time resolved FRET measurements are discussed.*Methods for Evaluating Cooperativity in a Dimeric Hemoglobin*Multiple-Binding of Ligands to a Linear Biopolymer*Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions*Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural and Kinetic Analysis

Analyzing Intermediate State Cooperativity in Hemoglobin; Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity; Evaluating Cooperativity in Dimeric Hemoglobins; Measuing Assembly and Binding in Human Embryonic Hemoglobins; Small-Angle Scattering Techniques for Analyzing; Conformational Transitions in Hemocyanins; Multivalent Protein-Carbohydrate Interactions: Isothermal Titration Microcalorimetry Studies; Calorimetric Analysis of Mutagenic Effects on Protein-Ligand Interactions; Multiple Binding of Ligands to a Linear Biopolymer; Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy; Fluorescence Quenching Methods to Study Protein-Nucleic Acid interactions; Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure-Function; Linked Equilibria in Biotin Repressor Function: Thermodynamics, Structural, and Kinetic Analysis; Distance Parameters Derived from Time-Resolved Förster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions