Elsevier S & T

Energetics of Biological Macromolecules, Part D

Holt, Jo M.; Johnson, Michael L.; Ackers, Gary K.

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Table of contents
  • Table of Contentsv
  • Contributors to Volume 379vii
  • Prefaceix
  • Volumes in Seriesxi
  • Section I: Cooperative Binding1
  • Chapter 1. Analyzing Intermediate State Cooperativity in Hemoglobin3
  • Chapter 2. Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity28
  • Chapter 3. Evaluating Cooperativity in Dimeric Hemoglobins55
  • Chapter 4. Measuring Assembly and Binding in Human Embryonic Hemoglobins64
  • Chapter 5. Small-Angle Scattering Techniques for Analyzing Conformational Transitions in Hemocyanins81
  • Chapter 6. Multivalent Protein–Carbohydrate Interactions: Isothermal Titration Microcalorimetry St107
  • Chapter 7. Calorimetric Analysis of Mutagenic Effects on Protein–Ligand Interactions128
  • Chapter 8. Multiple Binding of Ligands to a Linear Biopolymer145
  • Chapter 9. Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and N152
  • Chapter 10. Fluorescence Quenching Methods to Study Protein–Nucleic Acid Interactions175
  • Chapter 11. Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose R188
  • Chapter 12. Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural, and Kinetic A209
  • Chapter 13. Distance Parameters Derived from Time- Resolved Fo¨ rster Resonance Energy Transfer Mea235
  • Author Index263
  • Subject Index275
Book details
  • Vendor Elsevier S & T
  • SKU 9780121827830
  • ISBN-13 9780080497174
  • Author Holt, Jo M.; Johnson, Michael L.; Ackers, Gary K.
  • Category Science
  • Subject Molecular Biology

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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