Molecular Dynamics Simulations of Prion Proteins- Effect of Ala117 →Val mutation-

Chem-Bio Informatics Journal

Kazunori Yamanaka²  Ryutaro Susukita⁴  Atsushi Kawai⁴  Hideaki Furusawa⁴  Tetsu Narumi³  Kenji Yasuoka¹  Atsushi Suenaga³  Toshikazu Ebisuzaki⁴  Tyuji Hoshino²  Noriaki Okimoto⁴  Masayuki Hata²  Noriyuki Futatsugi³  Takahiro Koishi⁴  Yoshinori Hirano⁴ 

[1] Keio University Department of Mechanical Engineering;Graduate School of Pharmaceutical Sciences, Chiba University;Genomic Sciences Center, Institute of Physical and Chemical Research (RIKEN);Advanced Computing Center, Computational Science Division, Institute of Physical and Chemical Research (RIKEN)

关键词: Molecular Dynamics Simulation;    分子動力学計算;    Prion Protein;    プリオンプロテイン;    Gerstmann-Straussler-Sheinker disease;    Gerstmann-Straussler-Sheinker症�?�群;    Molecular Dynamics Machine;    分子動力学専用計算機（MDM）;   

DOI  :  10.1273/cbij.3.1

学科分类：生物化学/生物物理

来源: Chem-Bio Informatics Society

【 摘 要 】

References(24)Cited-By(8)We investigated the conformational change in the human prion protein owing to an 117 →Val mutation by using molecular dynamics simulations. This mutation is related to Gerstmann-Sträussler-Sheinker disease, one of the familial prion diseases. Five prion protein structures were simulated in the periodic or non-periodic system. The results of molecular dynamics calculations indicated that the globular domains of wild-type structures (109-228 and 90-228) were stable. In contrast, the globular domains of mutant structures (109-228 and 90-228) were sensitive to the N-terminal region possessing the Ala117 →Val mutation, and the ß-sheet regions were increased.

【 授权许可】

Unknown