Neutron Protein Crystallography: Beyond the Folding Structure

Journal Article · Mon Mar 17 04:00:00 EDT 2008 · AIP Conference Proceedings

DOI:https://doi.org/10.1063/1.2906091· OSTI ID:21136860

Niimura, N ^[1]

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1. Institute of Applied Beam Science, Graduate School of Science and Engineering, Ibaraki University, 4-12-1 Naka-Narusawa, Hitachi, Ibaraki 316-8511 (Japan)

Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins, a technique complementary to ultra-high-resolution X-ray diffraction. A neutron diffractometers for biological macromolecules has been constructed in Japan, and it has been used to determine the crystal structures of proteins up to resolution limits of 1.5-2.5 A. Results relating to hydrogen positions and hydration patterns in proteins have been obtained from these studies. Examples include the geometrical details of hydrogen bonds, the role of hydrogen atoms in enzymatic activity, CH{sub 3} configuration, H/D exchange in proteins and oligonucleotides, and the dynamical behavior of hydration structures, all of which have been extracted from these structural results and reviewed.

• OSTI ID: 21136860
• Journal Information: AIP Conference Proceedings, Journal Name: AIP Conference Proceedings Journal Issue: 1 Vol. 989; ISSN APCPCS; ISSN 0094-243X
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
HYDRATION
HYDROGEN
JAPANESE ORGANIZATIONS
NEUTRON DIFFRACTION
NEUTRONS
OLIGONUCLEOTIDES
PROTEINS
RESOLUTION
STRUCTURAL CHEMICAL ANALYSIS
X-RAY DIFFRACTION