Molecular Dynamics Studies of the Bufallo Prion Protein Structured Region at Higher Temperatures

Molecular dynamics (MD) studies of buffalo prion protein (BufPrP$^\text{C}$) [Zhang JP et al.(2016) J Biomol Struct Dyn 34(4):762-777] showed that the structure of this protein is very stable at room temperature (whether under neutral pH or low pH environments). In order to understand the reason why buffalo is lowly susceptible to prion diseases and why BufPrP$^\text{C}$ is so stable at room temperature, this paper will prolong our MD running time at room temperature and extend our research to higher temperatures to study this BufPrP$^\text{C}$ structure furthermore. From the salt bridge point of view we found an important reason why BufPrP$^\text{C}$ is so stable at room temperature and this might be a nice clue of drug discovery or drug design for the treatment of prion diseases.

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