A MOLECULAR DYNAMICS SIMULATION STUDY OF CONFORMATIONAL CHANGES AND SOLVATION OF Aβ PEPTIDE IN TRIFLUOROETHANOL AND WATER
2009 ◽
Vol 08
(02)
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pp. 215-231
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Keyword(s):
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.
2019 ◽
Vol 578
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pp. 123613
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2008 ◽
Vol 112
(10)
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pp. 2888-2900
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2013 ◽
Vol 12
(08)
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pp. 1341015
2013 ◽
Vol 15
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Vol 17
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1995 ◽
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2009 ◽
Vol 352
(1-3)
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pp. 99-102
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