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- W2051235433 abstract "The secondary conformational change of cellular prion protein (PrPc) into scrapie prion protein (PrPsc) is critical important for prion disease including bovine spongiform encephalopathy and Creutzfeldt-Jakob disease.This study performed molecular dynamics simulations of both human prion protein (WT-PrPc) and pathogenic mutant prion protein (T188R) and analyze its conserved water molecules in equilibrium state.Although the secondary structure is not dramatically different, increase of Cα- RMSF occurs not only around mutation point but also in a wide range. This increase of intensity may result from the instability caused by point mutation.Next, we calculated mean residence time for each protein atoms to find conserved water molecules. Residence time is defined that the time from when the water molecule get into the sphere whose center is a protein atom to the evacuation of water molecule from the sphere. We found four conserved water molecule sites in WT-PrPc. Conserved water molecules also keep the higher rotational correlation than water molecules in bulk. These results shows that conserved water molecules are not only wrapped but also fixed by hydrogen bond between conserved water molecule and amino acids.On the other hand, every residence time of T188R decrease compared by WT-PrPc and the rotational relaxation is also faster than WT-PrPc although secondary structure is almost not different. These results show that conserved water molecules cannot survive related to the wide range fluctuation caused by point mutation." @default.
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- W2051235433 date "2014-01-01" @default.
- W2051235433 modified "2023-09-26" @default.
- W2051235433 title "Molecular Dynamics Study of Conserved Water Molecules in PrPc and Pathological Point Mutation T188R" @default.
- W2051235433 doi "https://doi.org/10.1016/j.bpj.2013.11.3383" @default.
- W2051235433 hasPublicationYear "2014" @default.
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