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Massive conformation change in the prion protein: Using dual-basin structure-based models to find misfolding pathways.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Singh, Jesse P. Whitford, Paul C. Hayre, N. R. Onuchic, José Cox, Daniel L.
Description	Country affiliation: United States Author Affiliation: Singh JP ( Department of Physics and the Institute for Complex Adaptive Matter, University of California at Davis, Davis, California 95616, USA. jsingh@physics.ucdavis.edu)
Abstract	We employ all-atom structure-based models with a force field with multiple energetic basins for the C-terminal (residues 166-226) of the mammalian prion protein. One basin represents the known alpha-helical ( H) structure while the other represents the same residues in a left-handed beta-helical (LHBH) conformation. The LHBH structure has been proposed to help describe one class of in vitro grown fibrils, as well as possibly self-templating the conversion of normal cellular prion protein to the infectious form. Yet, it is unclear how the protein may make this global rearrangement. Our results demonstrate that the conformation changes are not strongly limited by large-scale geometry modification and that there may exist an overall preference for the LHBH conformation. Furthermore, our model presents novel intermediate trapping conformations with twisted LHBH structure.
File Format	HTM / HTML
ISSN	08873585
Issue Number	5
Volume Number	80
e-ISSN	10970134
Journal	Proteins: Structure, Function, and Bioinformatics
Language	English
Publisher	Wiley-Liss
Publisher Date	2012-05-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Research Support, U.s. Gov't, Non-p.h.s. Chemistry Prions Humans Disulfides Discipline Biochemistry Protein Conformation Protein Stability Metabolism Molecular Dynamics Simulation Protein Folding Journal Article
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry Molecular Biology

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