A comparative molecular dynamics study on thermostability of human and chicken prion proteins.
To compare the thermostabilities of human and chicken normal cellular prion proteins (HuPrP(C) and CkPrP(C)), molecular dynamics (MD) simulations were performed for both proteins at an ensemble level (10 parallel simulations at 400 K and 5 parallel simulations at 300 K as a control). It is found that the thermostability of HuPrP(C) is comparable with that of CkPrP(C), which implicates that the non-occurrence of prion diseases in non-mammals cannot be completely attributed to the thermodynamic properties of non-mammalian PrP(C).
Ji
Hong-Fang
HF
Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Center for Advanced Study, Shandong University of Technology, Zibo 255049, PR China.
Zhang
Hong-Yu
HY
D000818:Animals; D002645:Chickens; D006801:Humans; D008958:Models, Molecular; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D013696:Temperature; D013816:Thermodynamics
D011328:Prions