Library Science

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 E and its companion volume, Part D. The reader will observe remarkable similarities among the wide range of experimental strategies employed, attesting to fundamental issues inherent in all cooperative systems.

Download Jo M. Holt, Michael L. Johnson, and Gary K. Ackers

Table of Contents

• Editors-In-Chief (Page ii)
  Contributors to Volume 380 (pp.ix-x )
  Preface (Page xi)
  Methods In Enzymology (pp.xiii-xxxiv )
  Contributions to the Catalytic Efficiency of Enzymes, and the Binding of Ligands to Receptors, from Improvements in Packing within Enzymes and Receptors (pp3-19)
  Dudley H. Williams , Elaine Stephens , Min Zhou and Rosa Zerella

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