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Report No.

The Contribution of the Japanese team; Neutron diffraction experiment of fully deuterated proteins, such as RNase A, insulin, myoglobin and so on

Niimura, Nobuo*; Tanaka, Ichiro*; Onishi, Yuki*; Ostermann, A.*; Kurihara, Kazuo; Honjo, Eijiro; Kuroki, Ryota; Futami, Junichiro*; Yamada, Hidenori*

Our goal is to develop new methods for determining macromolecular crystal structures ${it ab initio}$ from neutron diffraction data and to validate these methods by making applications to several proteins. The proposed methods, which have the potential to be more powerful than X-ray ones, exploit perfectly isomorphous pairs of crystals that differ by replacement of D atoms with H atoms in selected amino-acid residues. This research involves collaboration among teams on three continents that have expertise in different aspects of neutron crystallography. The Japanese team measures high-resolution neutron diffraction data from protein crystals to answer questions about H bonding, protonation, hydration, and enzyme mechanisms. The team will focus on fundamental and simple proteins such as myoglobin, insulin, and RNase A at the first stage and then on rubredoxin, aldose reductase and other samples from the French team. In the meeting the research plan of the Japanese team will be reported.



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