Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1676529 | Thin Solid Films | 2006 | 5 Pages |
Abstract
The single point mutation F198S in prion protein can induce aberrant 3-dimensional structure which finally lead to serious disease. One of the most significant differences between normal and abnormal structures is the concentration of α-helix and β-sheet. By employing molecular dynamics method, we studied the structural transition induced by the mutation F198S. Our results show that the loss of the hydrophobic interactions between the 198-th residue and its surroundings may lead to the transition. A creation of additional β-sheet is captured in our investigation which has not been reported in the dynamical studies of mutated induced structure conversion in prion protein.
Related Topics
Physical Sciences and Engineering
Materials Science
Nanotechnology
Authors
Yong Zhang, Luru Dai, Mitsumasa Iwamoto, Zhong-can Ou-Yang,