Energetics of biological macromolecules. Part D [electronic resource] / edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers.
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TextSeries: Methods in enzymology ; v. 379.Publication details: Amsterdam ; Boston : Elsevier/Academic Press, �2004. Description: 1 online resource (xxxii, 281 pages, [4] pages of plates) : illustrations (some color)Content type: text Media type: computer Carrier type: online resourceISBN: 9780080497174 (electronic bk.); 0080497179 (electronic bk.); 0121827836 (electronic bk.); 9780121827830 (electronic bk.); 1281011460; 9781281011466Subject(s): Macromolecules | Bioenergetics | Cooperative binding (Biochemistry) | Allosteric proteins | Thermodynamics | Energy Metabolism | Macromolecular Systems | Thermodynamics | SCIENCE -- Life Sciences -- Biochemistry | Allosteric proteins | Bioenergetics | Cooperative binding (Biochemistry) | Macromolecules | ThermodynamicsGenre/Form: Electronic books.Additional physical formats: Print version:: Energetics of biological macromolecules. Part D.DDC classification: 572/.7 LOC classification: QP601 | .M49eb vol. 379Online resources: ScienceDirect | ScienceDirect Includes bibliographical references and indexes.
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.
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.
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