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. The key features include: 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; and, Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural and Kinetic Analysis.
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