Energetics of biological macromolecules. Part D /

• Άλλοι συγγραφείς: Holt, Jo M., Johnson, Michael L., 1947-, Ackers, Gary K.
• Μορφή: Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: Amsterdam ; Boston : Elsevier/Academic Press, ©2004.
• Σειρά: Methods in enzymology ; v. 379.
• Θέματα: Macromolecules.; Bioenergetics.; Cooperative binding (Biochemistry); Allosteric proteins.; Thermodynamics.; SCIENCE > Life Sciences > Biochemistry.; Macromolecular Substances [MESH]; Enzymes [MESH]; Protein Folding [MESH]; Electronic books.

 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. 

 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.