Dresden 2003 – wissenschaftliches Programm
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CPP: Chemische Physik und Polymerphysik
CPP 3: Biomoleküle
CPP 3.6: Vortrag
Montag, 24. März 2003, 11:30–11:45, ZEU/118
Light-triggered conformational transition of a cyclic peptide monitored by ultrafast vibrational spectroscopy — •Jens Bredenbeck1, Jan Helbing1, Arne Sieg2, Tobias Schrader2, Wolfgang Zinth2, Christian Renner3, Raymond Behrendt3, Luis Moroder3, Josef Wachtveitl4 und Peter Hamm1 — 1Physikalisch Chemisches Institut, Universität Zürich, Winterthurer Strasse 190, CH-8057 Zürich, Schweiz — 2Ludwig-Maximilians-Universität München, Lehrstuhl für BioMolekulare Optik, Oettingenstrasse 67, 80538 München, Germany — 3Max-Planck Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany — 4Johann Wolfgang Goethe Universität Frankfurt am Main, Institut für Physikalische und Theoretische Chemie, Marie-Curie-Strasse 11, D-60439 Frankfurt am Main, Germany
We use ultrafast IR spectroscopy to monitor the nonequilibrium backbone dynamics of a cyclic petide in the amide-I range. A conformational change of the peptide is induced by means of a photo-isomerizable pseudo amino acid integrated into the peptide backbone. Even though the main conformational change of the backbone is complete after 20 ps, we observe continued dynamics extending into the ns range. This is discussed in the context of relaxation of the dihedral angles of the backbone adjusting to the stretched overall structure, which the petide aquires after isomerization of the photoswitch. The aspects and prospects of using 2D IR experiments to monitor nonequilibrium structural dynamics of peptides are discussed.