title: Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules.
abstract: 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.
authors.affiliation: Science Directorate, European Spallation Source ERIC, Tunavägen 24, 22100 Lund, Sweden. esko.oksanen@esss.se.|Department of Biochemistry and Structural Biology, Lund University, Sölvegatan 39, 22362 Lund, Sweden. esko.oksanen@esss.se.
authors.forename: Esko
authors.initials: E
authors.lastname: Oksanen
authors.affiliation: Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. chen_j@lanl.gov.
authors.forename: Julian C-H
authors.initials: JC
authors.lastname: Chen
authors.affiliation: Science Directorate, European Spallation Source ERIC, Tunavägen 24, 22100 Lund, Sweden. zoe.fisher@esss.se.|Department of Biology, Lund University, Sölvegatan 35, 22362 Lund, Sweden. zoe.fisher@esss.se.
authors.forename: Suzanne Zoë
authors.initials: SZ
authors.lastname: Fisher
mesh_terms: D018360:Crystallography, X-Ray; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D006878:Hydroxides / Q000737:chemistry; D008024:Ligands; D046911:Macromolecular Substances / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D009502:Neutrons; D009861:Onium Compounds / Q000737:chemistry; D010084:Oxidation-Reduction; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D012997:Solvents / Q000737:chemistry; D013379:Substrate Specificity; D014867:Water / Q000737:chemistry
chemical_list: D004798:Enzymes; D006878:Hydroxides; D008024:Ligands; D046911:Macromolecular Substances; D009861:Onium Compounds; D011506:Proteins; D012997:Solvents; D014867:Water; C027727:hydronium ion; D006859:Hydrogen; C031356:hydroxide ion
keywords: hydrogen bond; neutron crystallography; nuclear density maps; solvent networks; structural enzymology