The effect of water on protein dynamics.

G Zaccai

Journal: Philosophical transactions of the Royal Society of London. Series B, Biological sciences 2004;359(1448):1269-75; discussion 1275, 1323-8

PMID: 15306381

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Abstract

Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.

Address: Institut de Biologie Structurale, 41 rue Jules Horowitz, Grenoble Cedex 1, France. [email protected]

DOI: 10.1098/rstb.2004.1503

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MeSH Terms: Bacteriorhodopsins, Euryarchaeota, Malate Dehydrogenase, Neutron Diffraction, Purple Membrane, Spectrum Analysis, Water