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Energetics of biological macromolecules. Part E / edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers.

Contributor(s): Material type: TextTextSeries: Methods in enzymology ; v. 380.Publication details: San Diego : Elsevier/Academic Press, ©2004.Description: 1 online resource (1 volume) : illustrations (some color)Content type:
  • text
Media type:
  • computer
Carrier type:
  • online resource
ISBN:
  • 9780080497181
  • 0080497187
  • 0121827844
  • 9780121827847
  • 1281011479
  • 9781281011473
Subject(s): Genre/Form: Additional physical formats: Print version:: Energetics of biological macromolecules. Part E.DDC classification:
  • 547/.7 22
LOC classification:
  • QD380 .E54eb pt. E
  • QP
Online resources:
Contents:
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.
Summary: 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.
Holdings
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Includes bibliographical references and indexes.

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.

Print version record.

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.

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