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Neutron crystallography for the study of hydrogen bonds in macromolecules

Oksanen, Esko LU ; Chen, Julian C.H. and Zoë Fisher, Suzanne (2017) In Molecules 22(4).
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... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Hydrogen bond, Neutron crystallography, Nuclear density maps, Solvent networks, Structural enzymology
in
Molecules
volume
22
issue
4
publisher
Molecular Diversity Preservation International
external identifiers
  • scopus:85019719728
  • wos:000404517800094
ISSN
1420-3049
DOI
10.3390/molecules22040596
language
English
LU publication?
yes
id
0ea2a031-5c0f-4760-be66-759c0835610e
date added to LUP
2017-07-04 07:27:39
date last changed
2017-09-24 05:12:50
@article{0ea2a031-5c0f-4760-be66-759c0835610e,
  abstract     = {<p>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.</p>},
  articleno    = {596},
  author       = {Oksanen, Esko and Chen, Julian C.H. and Zoë Fisher, Suzanne},
  issn         = {1420-3049},
  keyword      = {Hydrogen bond,Neutron crystallography,Nuclear density maps,Solvent networks,Structural enzymology},
  language     = {eng},
  month        = {04},
  number       = {4},
  publisher    = {Molecular Diversity Preservation International},
  series       = {Molecules},
  title        = {Neutron crystallography for the study of hydrogen bonds in macromolecules},
  url          = {http://dx.doi.org/10.3390/molecules22040596},
  volume       = {22},
  year         = {2017},
}