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Hydration in proteins observed by high‐resolution neutron crystallography
Author(s) -
Chatake Toshiyuki,
Ostermann Andreas,
Kurihara Kazuo,
Parak Fritz G.,
Niimura Nobuo
Publication year - 2003
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10303
Subject(s) - rubredoxin , crystallography , hydrogen bond , molecule , chemistry , myoglobin , neutron diffraction , resolution (logic) , intermolecular force , protein structure , neutron , chemical physics , crystal structure , physics , biochemistry , organic chemistry , quantum mechanics , artificial intelligence , computer science
It is well known that water molecules surrounding a protein play important roles in maintaining its structural stability. Water molecules are known to participate in several physiological processes through the formation of hydrogen bonds. However, the hydration structures of most proteins are not known well at an atomic level at present because X‐ray protein crystallography has difficulties to localize hydrogen atoms. In contrast, neutron crystallography has no problem in determining the position of hydrogens with high accuracy.1 In this article, the hydration structures of three proteins are described— myoglobin, wild‐type rubredoxin, and a mutant rubredoxin—the structures of which were solved at 1.5‐ or 1.6‐Å resolution by neutron structure determination. These hydration patterns show fascinating features and the water molecules adopt a variety of shapes in the neutron Fourier maps, revealing details of intermolecular hydrogen bond formation and dynamics of hydration. Our results further show that there are strong relationships between these shapes and the water environments. Proteins 2003;50:516–523. © 2003 Wiley‐Liss, Inc.