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Molecules 2017, 22(4), 596;

Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules

Science Directorate, European Spallation Source ERIC, Tunavägen 24, 22100 Lund, Sweden
Department of Biochemistry and Structural Biology, Lund University, Sölvegatan 39, 22362 Lund, Sweden
Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA
Department of Biology, Lund University, Sölvegatan 35, 22362 Lund, Sweden
Author to whom correspondence should be addressed.
Academic Editor: Steve Scheiner
Received: 12 March 2017 / Revised: 29 March 2017 / Accepted: 1 April 2017 / Published: 7 April 2017
(This article belongs to the Special Issue Intramolecular Hydrogen Bonding 2017)
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Abstract: The hydrogen bond (H bond) is one of the most important interactions that form the foundation of secondary and tertiary protein structure. Beyond holding protein structures together, H bonds are also intimately involved in solvent coordination, ligand binding, and enzyme catalysis. The H bond by definition involves the light atom, H, and it is very difficult to study directly, especially with X-ray crystallographic techniques, due to the poor scattering power of H atoms. Neutron protein crystallography provides a powerful, complementary tool that can give unambiguous information to structural biologists on solvent organization and coordination, the electrostatics of ligand binding, the protonation states of amino acid side chains and catalytic water species. The method is complementary to X-ray crystallography and the dynamic data obtainable with NMR spectroscopy. Also, as it gives explicit H atom positions, it can be very valuable to computational chemistry where exact knowledge of protonation and solvent orientation can make a large difference in modeling. This article gives general information about neutron crystallography and shows specific examples of how the method has contributed to structural biology, structure-based drug design; and the understanding of fundamental questions of reaction mechanisms. View Full-Text
Keywords: hydrogen bond; neutron crystallography; structural enzymology; nuclear density maps; solvent networks hydrogen bond; neutron crystallography; structural enzymology; nuclear density maps; solvent networks

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Oksanen, E.; Chen, J.-H.; Fisher, S.Z. Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules. Molecules 2017, 22, 596.

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