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Evaluation of Molecular Perturbation of a Deuterated Protein by Temperature Factor Refinement in X-Ray Structural Analysis of High- Resolution Diffraction Data
Takuya Uemura1,2, Akiko Kita2 and Yukio Morimoto2*1Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan
2Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan
- Corresponding Author:
- Yukio Morimoto
Division of Quantum Beam Material Science
Research Reactor Institute, Kyoto University
Kumatori, Osaka 590-0494, Japan
Tel: +81-72-451-237
Fax: +81-72-451-2371
E-mail: morimoto@rri.kyoto-u.ac.jp
Received date: April 09, 2016; Accepted date: April 21, 2016; Published date: April 28, 2016
Citation: Uemura T, Kita A, Morimoto Y (2016) Evaluation of Molecular Perturbation of a Deuterated Protein by Temperature Factor Refinement in X-Ray Structural Analysis of High-Resolution Diffraction Data. J Biotechnol Biomater 6:223. doi:10.4172/2155-952X.1000223
Copyright: © 2016 Uemura T, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Structural analysis of deuterated proteins, which are essential for neutron protein crystallography, involves refinement of X-ray crystallographic data using atomic or molecular thermal stability factors. Analysis of high resolution (~0.9 Å) X-ray data can localize some of the hydrogen atoms in a protein molecule. Thermal stabilities and temperature factors are affected by some reasons; one of them is the masses of hydrogen and deuterium atoms. We propose a method to refine X-ray data, taking into account these effects, to show existence probability for deuterium in the protein. Thermal factors were calculated using several physical parameters, and the resultant values were fitted to the experimental thermal factors with high accuracy. This computational method can be applied to analyze and predict the hydrogen/deuterium exchanged states of protein crystals, even small crystals that are unsuitable for neutron crystallography.
