- Title
- Studies on the structural stability of rabbit prion probed by molecular dyanamics simulations of its wild-type and mutants
- Creator
- Zhang, Jiapu
- Date
- 2010
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/59731
- Identifier
- vital:5205
- Identifier
- ISSN:0022-5193
- Abstract
- Prion diseases are invariabiably fatal and highly infectious neurodegenerative diseases that affect humans and animals. Rabbits are the only mammalian species reported to be resistant to infection from prion diseases isolated from other species (Vorber et.al., 2003). Fortunately, the NMR structure of rabbit prion (124-228) (PDB entry 2FJ3), the NMR structure of rabbit prion protein mutation s173N (PDB entry 2JOH) and the NMR structure of rabbit prion protein I214V [PDB entry 2JOM} were released recently. This paper studies these NMR structures by molecular dyanmaics simulations. Simulation results confirm the structural ability of wild-type rabbit prion, and show that the salt bridge between D177 and R163 greatly contributes to the structural stability of rabbity prion. Crown Copyright Published by Elsevier.
- Relation
- Journal of Theoretical Biology Vol. 264, no. (2010), p. 119-122
- Rights
- Copyright Crown Content
- Rights
- This metadata is freely available under a CCO license
- Subject
- 01 Mathematical Sciences; 06 Biological Sciences; 08 Information and Computing Sciences; Prion diseases; Immunity; Rabbit prion; Molecular dynmaics
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