| Full text | |
| Author(s): |
Total Authors: 2
|
| Affiliation: | [1] Univ Sao Paulo, FFCLRP, Dept Fis, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil
[2] Univ Tecnol Fed Parana, Rua Cristo Rei 19, BR-85902490 Toledo, PR - Brazil
Total Affiliations: 2
|
| Document type: | Journal article |
| Source: | Journal of Physical Chemistry B; v. 122, n. 6, p. 1869-1875, FEB 15 2018. |
| Web of Science Citations: | 3 |
| Abstract | |
Structural properties of A beta(16-35) fragment are investigated as a model for the amyloid-beta peptide excluding its coil-inducing terminals. Our replica-exchange molecular dynamics simulations using all-atom and explicit aqueous solvation widely reduce any structural bias. The principal folding pathway shows direct conversion of coil to beta-sheet, without the long proposed helix intermediates. Our principal component analysis indicates that the fragment is also intrinsically disordered, as the full amyloid-beta peptide. Thus, the observed folding mechanism lacks free-energy barriers and any peaks in the thermal capacity. (AU) | |
| FAPESP's process: | 16/04176-4 - Systematic analysis in silico of the critical behavior of amyloid beta peptide and some of its mutants |
| Grantee: | Nelson Augusto Alves |
| Support Opportunities: | Regular Research Grants |