UID:
almafu_9958132557102883
Umfang:
1 online resource (315 p.)
ISBN:
9786611011468
,
9781281011466
,
1281011460
,
9780080497174
,
0080497179
Serie:
Methods in enzymology, v. 379
Inhalt:
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.*Methods for Evaluating Cooperativity in a Dimeric Hemoglobin*Multiple-Binding of Ligands to a Linear Biopolymer*Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions*Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural and Kinetic Analysis
Anmerkung:
Description based upon print version of record.
,
Front Cover; Energetics of Biological Macromolecules; Copyright Page; Table of Contents; Contributors to Volume 379; Preface; Volumes in Series; Section I: Cooperative Binding; Chapter 1. Analyzing Intermediate State Cooperativity in Hemoglobin; Chapter 2. Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity; Chapter 3. Evaluating Cooperativity in Dimeric Hemoglobins; Chapter 4. Measuring Assembly and Binding in Human Embryonic Hemoglobins; Chapter 5. Small-Angle Scattering Techniques for Analyzing Conformational Transitions in Hemocyanins
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Chapter 6. Multivalent Protein-Carbohydrate Interactions: Isothermal Titration Microcalorimetry StudiesChapter 7. Calorimetric Analysis of Mutagenic Effects on Protein-Ligand Interactions; Chapter 8. Multiple Binding of Ligands to a Linear Biopolymer; Chapter 9. Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy; Chapter 10. Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions
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Chapter 11. Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure-FunctionChapter 12. Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural, and Kinetic Analysis; Chapter 13. Distance Parameters Derived from Time- Resolved Fo ̈ rster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions; Author Index; Subject Index
,
English
Weitere Ausg.:
ISBN 9780121827830
Weitere Ausg.:
ISBN 0121827836
Sprache:
Englisch
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