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Light-triggered β-hairpin folding and unfolding
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Journal Article
Light-triggered β-hairpin folding and unfolding
2007
Overview
A light-switchable peptide is transformed with ultrashort pulses from a β-hairpin to an unfolded hydrophobic cluster and vice versa. The structural changes are monitored by mid-IR probing. Instantaneous normal mode analysis with a Hamiltonian combining density functional theory with molecular mechanics is used to interpret the absorption transients. Illumination of the β-hairpin state triggers an unfolding reaction that visits several intermediates and reaches the unfolded state within a few nanoseconds. In this unfolding reaction to the equilibrium hydrophobic cluster conformation, the system does not meet significant barriers on the free-energy surface. The reverse folding process takes much longer because it occurs on the time scale of 30 μs. The folded state has a defined structure, and its formation requires an extended search for the correct hydrogen-bond pattern of the β-strand.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
