This is the first book covering all aspects of high pressure biochemistry and biophysics of proteins.
Hydrostatic pressure is a powerful tool for study of biological systems. As a thermodynamic parameter, hydrostatic pressure has been known for a century to act on biological materials in a similar, but not identical, way to temperature. However, pressure was disregarded for a long time by biochemists mainly because the basic concepts (and the thermodynamics) focused on the chemical reactions involved and because general ideas on what pressure can add to the understanding of the behaviour of proteins were lacking. In recent decades, technological progress in the field of physics has shown, along with parameters such as temperature and solvent conditions, that pressure can be used for more refined thermodynamic and kinetic descriptions of biological processes and regulation of biological systems. The effects of pressure on proteins, nucleoproteins and membranes have recently been reviewed and several proceedings books have been published.
Preface. I. Introduction. High pressure effects on biological macromolecules: From structural changes to alteration of cellular processes (C. Balny et al.). II. Revisiting some basic concepts. Pressure-temperature phase diagrams of biomolecules (L. Smeller). The effects of osmotic and hydrostatic pressures on macromolecular systems (J.A. Kornblatt, M.J. Kornblatt). Compressibility of protein transitions (N. Taulier, T.V. Chalikian). Effects of high pressure on enzymatic activity (D.B. Northrop). III. Major developments in experimental methodology. UV-Visible derivative spectroscopy under high pressure (R. Lange, C. Balny). High pressure static fluorescence to study macromolecular structure-function (K. Ruan, C. Balny). Investigations of the effect of high hydrostatic pressure on proteins and lipidic membranes by dynamic fluorescence spectroscopy (P. Tauc et al.). Tryptophan phosphorescence and pressure effects on protein structure (P. Cioni, G.B. Strambini). Fourier transform infrared spectroscopy in high pressure studies on proteins (W. Dzwolak et al.). High resolution NMR studies of proteins (J. Jonas). Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure (R. Winter). High pressure simulations of biomolecules (E. Paci).IV. Folding, unfolding and molecular interactions : the high pressure approach. Revisiting volume changes in pressure-induced protein unfolding (C.A. Royer). Expanding the pressure technique: Insights into protein folding from combined use of pressure and chemical denaturants (S. Perrett, J.-M. Zhou). High hydrostatic pressure as a tool to study protein aggregation and amyloidosis (T.W. Randolph et al.). Pressure effects on intra- and intermolecular interactions within proteins (B.B. Boonyaratanakornkit et al.). Pressure induces folding intermedia
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- © Elsevier Science 2002
- 5th June 2002
- Elsevier Science
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Department of Chemistry, KUL, Celestijnenlaan 200 D, B-3001 Leuven, Belgium
CRSSA, Dept. Toxicology, Enzymology Unit, BP 87, F-38702 La Tronche Cedex, France