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BioMed Research International
Volume 2017, Article ID 4184106, 8 pages
Research Article

Effect of R119G Mutation on Human P5CR1 Dynamic Property and Enzymatic Activity

1Laboratory of Molecular Cardiology, Department of Cardiology, The First Affiliated Hospital of Kunming Medical University, Kunming, China
2Department of Computer Science, The Faculty of Basic Medicine, Kunming Medical University, Kunming, China

Correspondence should be addressed to Zhaohui Meng; moc.nuyila@gnemhhz

Received 3 October 2016; Revised 13 December 2016; Accepted 29 December 2016; Published 18 January 2017

Academic Editor: Luis Loura

Copyright © 2017 Linhua Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

The 3D structures of the R119G and R119H mutants were nearly identical to WT. (A) WT; (B) R119G; mutagenesis of Arginine 119 to Glycine (C) R119H; mutagenesis of Arginine 119 to Histidine

  1. Supplementary Material