Characterizing the denatured state of human prion 121-230

Biophysical Chemistry
Cheng-I Lee, Nai-yuan Chang

Abstract

Misfolding and aggregation of the prion protein (PrP) are responsible for the development of fatal transmissible neurodegenerative diseases. PrP undergoes structural conversion from a natively folded state into a misfolded state, resulting in insoluble amyloid fibrils. Partial unfolding has been recognized as an essential step in fibrillation. The strong correlation of unfolding and fibrillation emphasizes the importance of denatured states. To gain insight into possible aggregation-prone denatured states, we characterized the denatured state of human prion (huPrP) 121-230 near extended conformation by self-guided Langevin dynamics simulations. Our results revealed that denatured huPrP is partially folded with alpha-helical structure.

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Citations

Dec 15, 2010·Journal of Biomolecular Structure & Dynamics·Sridevi Akella, Chanchal K Mitra
Sep 6, 2013·International Journal of Molecular Sciences·Shen-Jie LinCheng-I Lee
Aug 3, 2012·The Journal of Chemical Physics·Xiongwu WuBernard R Brooks
Apr 12, 2011·The Journal of Chemical Physics·Xiongwu Wu, Bernard R Brooks
Nov 15, 2011·Biochimie·Swagata ChakrabortyRamakrishna V Hosur
Jul 18, 2015·Journal of Computational Chemistry·Xiongwu WuEric Vanden-Eijnden
Sep 7, 2020·The Journal of Chemical Physics·Xiongwu Wu, Bernard R Brooks
Oct 12, 2018·Journal of the American Chemical Society·Thomas E MorrellJhih-Wei Chu

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