*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
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.
Biochemists, biophysicists, bioengineers, molecular biologists, structural biologists
Energetics of Biological Macromolecules, Part D, 1st Edition
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
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