Ou-Yang, ZC , Chinese Acad Sci, Interdisciplinary Ctr Theoret Studies, POB 2735, Beijing 100864, Peoples R China
部门归属:
Chinese Acad Sci, Interdisciplinary Ctr Theoret Studies, Beijing 100864, Peoples R China; Chinese Acad Sci, Inst Theoret Phys, Beijing 100080, Peoples R China; Tokyo Inst Technol, Dept Phys Elect, Meguro Ku, Tokyo 1528552, Japan; Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China
英文摘要:
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 alpha-helix and beta-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 beta-sheet is captured in our investigation which has not been reported in the dynamical studies of mutated induced structure conversion in prion protein. (c) 2005 Elsevier B.V All rights reserved.
Yong, Y,Dai, LR,Iwamoto, M,et al. Molecular dynamics study on the conformational transition of prion induced by the point mutation: F198S[J]. THIN SOLID FILMS,2006,499(40910):224-228.
