Energetics of Biological Macromolecules, Part D

Edited by

  • Jo Holt, Washington University Medical Center, St. Louis, MO, USA
  • Michael Johnson, University of Virginia Health Sciences Center, Charlottesville, USA
  • Gary Ackers, Washington University School of Medicine, St. Louis, Mo, USA

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.
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Biochemists, biophysicists, bioengineers, molecular biologists, structural biologists


Book information

  • Published: March 2004
  • ISBN: 978-0-12-182783-0


"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." CHEMISTRY IN INDUSTRY

Table of Contents

Analyzing Intermediate State Cooperativity in Hemoglobin; Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity; Evaluating Cooperativity in Dimeric Hemoglobins; Measuing Assembly and Binding in Human Embryonic Hemoglobins; Small-Angle Scattering Techniques for Analyzing; Conformational Transitions in Hemocyanins; Multivalent Protein-Carbohydrate Interactions: Isothermal Titration Microcalorimetry Studies; Calorimetric Analysis of Mutagenic Effects on Protein-Ligand Interactions; Multiple Binding of Ligands to a Linear Biopolymer; Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy; Fluorescence Quenching Methods to Study Protein-Nucleic Acid interactions; Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure-Function; Linked Equilibria in Biotin Repressor Function: Thermodynamics, Structural, and Kinetic Analysis; Distance Parameters Derived from Time-Resolved Förster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions