- Title
- Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions
- Creator
- Zhang, Jiapu; Wang, Feng; Zhang, Yuanli
- Date
- 2015
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/77062
- Identifier
- vital:7678
- Identifier
-
https://doi.org/10.1080/07391102.2014.947325
- Identifier
- ISSN:0739-1102
- Abstract
- Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and goats, cattle, deer and elk, and humans. But for rabbits, studies have shown that they have a low susceptibility to be infected by prion diseases. This paper does molecular dynamics (MD) studies of rabbit NMR structures (of the wild type and its two mutants of two surface residues), in order to understand the specific mechanism of rabbit prion proteins (RaPrPC). Protein surface electrostatic charge distributions are specially focused to analyze the MD trajectories. This paper can conclude that surface electrostatic charge distributions indeed contribute to the structural stability of wild-type RaPrPC; this may be useful for the medicinal treatment of prion diseases.
- Relation
- Journal of Biomolecular Structure and Dynamics Vol. 33, no. 6 (2015), p. 1326-1335
- Rights
- Copyright Taylor and Francis
- Rights
- This metadata is freely available under a CCO license
- Subject
- Molecular dynamics study; NMR structures; Prion diseases; Rabbit prion protein wild type and mutants; Surface electrostatic charge distributions; 0601 Biochemistry and Cell Biology
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