The effect of water on protein dynamics.
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.
Institut de Biologie Structurale, 41 rue Jules Horowitz, Grenoble Cedex 1, France. zaccai@ibs.fr
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D001436:Bacteriorhodopsins / Q000378:metabolism; D019605:Euryarchaeota / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D033363:Neutron Diffraction; D018717:Purple Membrane / Q000378:metabolism*; D013057:Spectrum Analysis; D014867:Water / Q000737:chemistry / Q000378:metabolism*
D014867:Water; D001436:Bacteriorhodopsins; D008291:Malate Dehydrogenase