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Relationship between population of the fibril-prone conformation in the monomeric state and oligomer formation times of peptides: Insights from all-atom simulations.
- Source :
- Journal of Chemical Physics; 4/28/2010, Vol. 132 Issue 16, p165104, 10p, 1 Diagram, 2 Charts, 8 Graphs
- Publication Year :
- 2010
-
Abstract
- Despite much progress in understanding the aggregation process of biomolecules, the factors that govern its rates have not been fully understood. This problem is of particular importance since many conformational diseases such as Alzheimer, Parkinson, and type-II diabetes are associated with the protein oligomerization. Having performed all-atom simulations with explicit water and various force fields for two short peptides KFFE and NNQQ, we show that their oligomer formation times are strongly correlated with the population of the fibril-prone conformation in the monomeric state. The larger the population the faster the aggregation process. Our result not only suggests that this quantity plays a key role in the self-assembly of polypeptide chains but also opens a new way to understand the fibrillogenesis of biomolecules at the monomeric level. The nature of oligomer ordering of NNQQ is studied in detail. [ABSTRACT FROM AUTHOR]
- Subjects :
- OLIGOMERS
PEPTIDES
PROTEINS
BIOMOLECULES
POLYPEPTIDES
LATTICE theory
Subjects
Details
- Language :
- English
- ISSN :
- 00219606
- Volume :
- 132
- Issue :
- 16
- Database :
- Complementary Index
- Journal :
- Journal of Chemical Physics
- Publication Type :
- Academic Journal
- Accession number :
- 50173825
- Full Text :
- https://doi.org/10.1063/1.3415372