Energetic of Biological Macromolecule Part D
posted in Enzymology |One of the most intriguing problems in biological energetics is that of cooperativity. From the discovery of cooperativity and allostery in hemoglobin 100 years ago (Bohr et al., 1904)1 to the characterization of cooperativity in a myriad of processes in modern times (i.e., transport, catalysis, signaling, assembly, folding), the molecular mechanisms by which energy is transferred from one part of a macromolecule to another continues to challenge us. Of course, the problem has many layers, as a molecule as ‘‘simple’’ and familiar as hemoglobin can simultaneously sense the chemical potential of each physiological ligand and adjust its interactions with the others accordingly. Ironically, the very allosteric intermediates that hold the structural and energetic secrets of cooperativity are the same whose populations are suppressed and, in many instances, largely obscured by the nature of cooperativity itself. Thus, innovative methodologies and techniques have been developed to address cooperative systems, many of which are presented in this volume Energetics of Biological Macromolecules Part D and its companion volume, Part E. The reader will observe remarkable similarities among the wide range of experimental strategies employed, attesting to fundamental issues inherent in all cooperative systems.
energetic-of-biological-macromolecule-part-d.pdf
Table of Contents
- Editors-In-Chief (Page ii)
- Contributors to Volume 379 (pp.vii-viii )
- Preface (Page ix)
- Methods In Enzymology (pp.xi-xxxii )
- Analyzing Intermediate State Cooperativity in Hemoglobin (pp3-28)
Gary K. Ackers , Jo M. Holt , E. Sethe Burgie and Connie S. Yarian - Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity (pp28-54)
Doug Barrick , Jonathan A. Lukin , Virgil Simplaceanu and Chien Ho - Evaluating Cooperativity in Dimeric Hemoglobins (pp55-64)
Alberto Boffi and Emilia Chiancone - Measuring Assembly and Binding in Human Embryonic Hemoglobins (pp64-80)
Thomas Brittain - Small-Angle Scattering Techniques for Analyzing Conformational Transitions in Hemocyanins (pp81-106)
Hermann Hartmann and Heinz Decker - Multivalent Protein–Carbohydrate Interactions: Isothermal Titration Microcalorimetry Studies (pp107-128)
Tarun K. Dam and C. Fred Brewer - Calorimetric Analysis of Mutagenic Effects on Protein–Ligand Interactions (pp128-145)
Frederick P. Schwarz - Multiple Binding of Ligands to a Linear Biopolymer (pp145-152)
Yi-der Chen - Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy (pp152-175)
Irina M. Russu - Fluorescence Quenching Methods to Study Protein–Nucleic Acid Interactions (pp175-187)
Siddhartha Roy - Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure–Function (pp188-209)
Liskin Swint-Kruse and Kathleen S. Matthews - Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural, and Kinetic Analysis (pp209-234)
Dorothy Beckett - Distance Parameters Derived from Time-Resolved Forster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein–DNA Interactions (pp235-262)
Lawrence J. Parkhurst
- Author Index (pp263-274 )
- Subject Index (pp275-281)