Energetics of biological macromolecules
By: edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers
Series: Methods in enzymology -- v. 379; Methods in enzymology -- v. 379.
Publisher: Elsevier/Academic Press
Published: 2004
Place of publication: San Diego
Language: eng
Number of pages: 281
Copyright date: 2004
Subjects: Macromolecules; Bioenergetics; Cooperative binding (Biochemistry); Allosteric proteins; Thermodynamics; Energy Metabolism; Macromolecular Substances
Notes: Includes bibliographical references and indexes.
Table of contents: title: 1. Analyzing intermediate state cooperativity in hemoglobin; title: 2. Nuclear magnetic resonance spectroscopy in the study of hemoglobin cooperativity; title: 3. Evaluating cooperativity in dimeric hemoglobins; title: 4. Measuring assembly and binding in human embryonic hemoglobins; title: 5. Small-angle scattering techniques for analyzing conformational transitions in hemocyanins; title: 6. Multivalent protein-carbohydrate interactions: isothermal titration microcalorimetry studies; title: 7. Calorimetric analysis of mutagenic effects on protein-ligand interactions; title: 8. Multiple binding of ligands to a linear biopolymer; title: 9. Probing site-specific energetics in proteins and nucleic acids by hydrogen exchange and nuclear magnetic resonance spectroscopy; title: 10. Fluorescence quenching methods to study protein-nucleic acid interactions; title: 11. Thermodynamics, protein modification, and molecular dynamics in characterizing lactose repressor protein: strategies for complex analyses of protein structure-function; title: 12. Linked equilibria in biotin repressor function: thermodynamic, structural and kinetic analysis; title: 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.