Article
Bulky side chains and non-native salt bridges slow down the folding of a cross-linked helical peptide: a combined molecular dynamics and time-resolved infrared spectroscopy study.
The journal of physical chemistry. B - 2 Apr 2009
Paoli Beatrice, Seeber Michele, Backus Ellen H G, Ihalainen Janne A, Hamm Peter, Caflisch Amedeo
Abstract excerpt
Multiple 4-micros molecular dynamics (MD) simulations are used to study the folding process of the cross-linked alpha-helical peptide Ac-EACAR(5)EAAAR(10)EAACR(15)Q-NH(2) (EAAAR peptide). The folding kinetics are single exponential at 330 K, while they are complex at 281 K with a clear deviation from single-exponential behavior, in agreement with time-resolved infrared (IR) spectroscopy measurements. Network...
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