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Energetics of biological macromolecules. Part D /

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.

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Holt, Jo M., Johnson, Michael L., 1947-, Ackers, Gary K.
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Amsterdam ; Boston : Elsevier/Academic Press, �2004.
Colección:Methods in enzymology ; v. 379.
Temas:
Acceso en línea:Texto completo
Texto completo

MARC

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245 0 0 |a Energetics of biological macromolecules.  |n Part D /  |c edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers. 
260 |a Amsterdam ;  |a Boston :  |b Elsevier/Academic Press,  |c �2004. 
300 |a 1 online resource (xxxii, 281 pages, 4 unnumbered pages of plates) :  |b illustrations (some color) 
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490 1 |a Methods in enzymology,  |x 0076-6879 ;  |v v. 379 
504 |a Includes bibliographical references and indexes. 
505 0 |a 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. 
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700 1 |a Holt, Jo M. 
700 1 |a Johnson, Michael L.,  |d 1947- 
700 1 |a Ackers, Gary K. 
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830 0 |a Methods in enzymology ;  |v v. 379.  |x 0076-6879 
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