Energetics of biological macromolecules. Part E /

This volume focuses on methods related to allosteric enzymes and receptors, including fluorescent proves, spectroscopic methods and quantitative analysis as well as on cooperativity in protein folding. NMR and mass spectrometry methods 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: San Diego : Elsevier/Academic Press, �2004.
Colección:Methods in enzymology ; v. 380.
Temas:
Macromolecules.
Bioenergetics.
Allosteric enzymes.
Protein folding.
Thermodynamics.
Energy metabolism.
Energy Metabolism
Macromolecular Systems
Protein Folding
Thermodynamics
Bio�energ�etique.
Enzymes allost�eriques.
Prot�eines > Repliement.
Thermodynamique.
M�etabolisme �energ�etique.
thermodynamics.
SCIENCE > Chemistry > Organic.
Energy metabolism
Allosteric enzymes
Bioenergetics
Macromolecules
Protein folding
Biof�isica.
Acceso en línea:Texto completo
Texto completo
Tabla de Contenidos:
  • 1. Contributions to the catalytic efficiency of enzymes, and the binding of ligands to receptors, from improvements in packing within enzymes and receptors
  • 2. Structural interpretation of pH and salt-dependent processes in proteins with computational methods
  • 3. Electrostatic basis for bioenergetics
  • 4. Local and global control mechanisms in allosteric threonine deaminase
  • 5. Methods for analyzing cooperativity in phosphoglycerate dehydrogenase
  • 6. Fluorescent probes applied to catalytic cooperativity in ATP synthase
  • 7. Measurement of energetics of conformational change in cobalamin-dependent methionine synthase
  • 8. Spectroscopic and kinetic methods for ligand-protein interactions of glutamate receptor
  • 9. Quantitative analysis and interpretation of allosteric behavior
  • 10. The immobilized template assay for measuring cooperativity in eukaryotic transcription complex assembly
  • 11. Characterization of the cargo attachment complex of cytoplasmic dynein using NMR and mass spectrometry
  • 12. Circular dichroism of protein-folding intermediates
  • 13. Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of staphylococcus aureus aldolase
  • 14. Kinetic and spectroscopic analysis of early events in protein folding
  • 15. Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding
  • 16. Cooperativity principles in protein folding
  • 17. Native state hydrogen-exchange analysis of protein folding and protein motional domains
  • 18. The preparations of ¹⁹F-labeled proteins for NMR studies.

Ejemplares similares