Abstract
The NMR structures of wild-type mouse PrPC PrP(119–232) at 37∘ C and mouse PrPC(124–226/121–232) at 20∘ C show characteristically different solvent-exposed epitopes near their β2-α2 loop . This Chapter does MD studies on these three mouse PrP structures determined at different temperature levels, in order to see different character near the β2-α2 loop and the structural performance of wild-type mousePrPC under long time of MD.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Damberger FF, Christen B, Pérez DR, Hornemann S, Wüthrich K (2011) Cellular prion protein conformation and function. Proc Natl Acad Sci USA 108(42):17308–17313
Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K (1996) NMR structure of the mouse prion protein domain PrP(121–231). Nature 382(6587):180–182
Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wüthrich K (1998) Prion protein NMR structure and familial human spongiform encephalopathies. Proc Natl Acad Sci USA 95(20):11667–11672
Zhang JP (2011c) Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins. J Theor Biol 269(1):88–95
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Zhang, J. (2018). Wild-Type Mouse 37 ∘C and 19.85 ∘C Structures. In: Molecular Dynamics Analyses of Prion Protein Structures. Focus on Structural Biology, vol 10. Springer, Singapore. https://doi.org/10.1007/978-981-10-8815-5_7
Download citation
DOI: https://doi.org/10.1007/978-981-10-8815-5_7
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-10-8814-8
Online ISBN: 978-981-10-8815-5
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)