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Recent results on hydrogen and hydration in biology studied by neutron macromolecular crystallography

Niimura, Nobuo; Arai, Shigeki; Kurihara, Kazuo; Chatake, Toshiyuki*; Tanaka, Ichiro*; Bau, R.*

Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins and DNA oligomers. Three different types of high resolution neutron diffractometers for biological macromolecules have been constructed in Japan, France and the U.S.A., and they have all been actively used in recent years to determine the crystal structures of numerous proteins. Examples include the detailed geometries of hydrogen bonds, information on H/D exchange in proteins, the unambiguous location of protons, the role of key hydrogen atoms in enzymatic activity and thermostability, and the dynamical behavior of hydration structures, all of which have been extracted from these structural results and reviewed in this article. Other important techniques, such as the optimization of growth of large single crystals using phase diagrams, the preparation of fully deuterated proteins, the introduction of cryogenic techniques to neutron protein crystallography, and the establishment of a "hydrogen and hydration in proteins" database, will also be described in this paper.

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Category:Biochemistry & Molecular Biology

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