LMU München
Fakultät für Physik



(c) 2002 BMO

"Light triggered β-hairpin folding and unfolding"
T. E. Schrader, W. J. Schreier, T. Cordes, F. O. Koller, G. Babitzki, R. Denschlag, C. Renner, S.-L. Dong, M. Löweneck, L. Moroder, P. Tavan, and W. Zinth
Proc. Natl. Acad. Sci. USA 104 (2007) 15729-15734.

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.

BMO authors (in alphabetic order):
Galina Babizki
Thorben Cordes
Robert Denschlag
Florian Koller
Tobias Schrader
Wolfgang Schreier
Paul Tavan
Wolfgang Zinth

Assoziierte Projekte:
Photoswitchable model peptides and their conformational dynamics
Peptide and protein folding
QM/MM hybrid descriptions of solutes in complex solvents


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Letzte Änderung: 2016-09-14 11:34