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A MOLECULAR DYNAMICS SIMULATION STUDY OF CONFORMATIONAL CHANGES AND SOLVATION OF Aβ PEPTIDE IN TRIFLUOROETHANOL AND WATER.
- Source :
- Journal of Theoretical & Computational Chemistry; Apr2009, Vol. 8 Issue 2, p215-231, 17p, 2 Diagrams, 5 Charts, 5 Graphs
- Publication Year :
- 2009
-
Abstract
- Molecular dynamics (MD) simulations of amyloid beta peptide have been performed in aqueous solutions of trifluoroethanol with different concentrations. The amount of α-helical secondary structure increases when going from pure water to trifluoroethanol-rich solutions. The conformation obtained in 40% (v/v) trifluoroethanol solution is very similar to the experimental observations of beta peptide in sodium dodecyl sulfate micelle. In this solution, the peptide has two helical segments connected through a looped region. The C-terminal helix of beta peptide unfolds in pure water. The effect of trifluoroethanol on peptide's secondary structure has been explained using the properties calculated from MD trajectories. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 02196336
- Volume :
- 8
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Journal of Theoretical & Computational Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 38903275
- Full Text :
- https://doi.org/10.1142/S0219633609004769