Biophysics and Physicobiology (Mar 2021)

Deuteration Aiming for Neutron Scattering

  • Aya Okuda,
  • Rintaro Inoue,
  • Ken Morishima,
  • Tomohide Saio,
  • Yasuhiro Yunoki,
  • Maho Yagi-Utsumi,
  • Hirokazu Yagi,
  • Masahiro Shimizu,
  • Nobuhiro Sato,
  • Reiko Urade,
  • Koichi Kato,
  • Masaaki Sugiyama

DOI
https://doi.org/10.2142/biophysico.bppb-v18.003
Journal volume & issue
Vol. 18

Abstract

Read online

The distinguished feature of neutron as a scattering probe is an isotope effect, especially the large difference in neutron scattering length between hydrogen and deuterium. The difference renders the different visibility between hydrogenated and deuterated proteins. Therefore, the combination of deuterated protein and neutron scattering enables the selective visualization of a target domain in the complex or a target protein in the multi-component system. Despite of this fascinating character, there exist several problems for the general use of this method: difficulty and high cost for protein deuteration, and control and determination of deuteration ratio of the sample. To resolve them, the protocol of protein deuteration techniques is presented in this report. It is strongly expected that this protocol will offer more opportunity for conducting the neutron scattering studies with deuterated proteins.

Keywords