Stuttgart 2012 – wissenschaftliches Programm
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MO: Fachverband Molekülphysik
MO 11: Biomolecules
MO 11.6: Vortrag
Dienstag, 13. März 2012, 15:15–15:30, V38.02
Light triggered peptide folding: Beta-hairpin formation on the nano to microsecond timescale. — •Andreas Deeg1, Michael Rampp1, Tobias E. Schrader1, Jose Pfizer2, Luis Moroder2, and Wolfgang Zinth1 — 1BioMolecular Optics, University of Munich, Germany — 2Max-Planck-Institut für Biochemie, Martinsried, Germany
The formation of secondary structure elements like alpha-helices or beta-hairpins are still a matter of intense scientific interest. We have investigated the folding mechanism of a beta-hairpin structure with a model peptide containing two amino acid strands connected by an azobenzene switch in the centre. The peptide forms a beta-hairpin when the azobenzene is in the cis conformation and a random structure for azobenzene in trans [1]. Recently the light triggered unfolding of the beta-hairpin has been investigated and the unfolding was observed within 3ns [2]. In this contribution the folding of the peptide was studied by time resolved vibrational spectroscopy on the nano to microsecond timescale for different temperatures. We observed strongly temperature dependent single exponential folding dynamics on the 10-100 microsecond timescale. A folding mechanism and an energy landscape, consistent with our data are discussed.
[1] S.-L Dong, Chem.Eur.J. 12, 1114-1120 (2006)
[2] T.E. Schrader, PNAS 104, 15729-15734 (2007)