Folding and Unfolding of Light-Triggered beta-Hairpin Model PeptidesSchrader, T. E., Cordes, T., Schreier, W. J., Koller, F. O., Dong, S-L., Moroder, L. & Zinth, W., 12-May-2011, In : The Journal of Physical Chemistry B. 115, 18, p. 5219-5226 8 p.
Research output: Contribution to journal › Article › Academic › peer-review
Ultrafast spectroscopy in the visible and mid-infrared is used to study the reaction dynamics of two light-triggered model peptides containing an azobenzene derivative as a switching element. One model peptide, the AzoTrpZip2, forms a beta-hairpin structure in the cis form of the chromophore. This peptide is compared to the core structure consisting of the chromophore and the two flanking amino acid residues, used as a minimal model. This combination of experiments performed in different spectral ranges on peptides of different sizes allows for improved insight into light triggered reaction dynamics. The kinetics observed for the core structure are directly connected to the switching process of the chromophore and are finished on the 10 Ps time scale. The trans-to-cis reaction of AzoTrpZip2, leading to the formation of the beta-hairpin structure involves ultrafast processes on the 100 ps time scale, which are directly related to the relaxation of the strain between the isomerized molecular switch and the two peptide strands. IR-signatures characteristic for changes in interstrand interactions are absent on the
|Number of pages||8|
|Journal||The Journal of Physical Chemistry B|
|Publication status||Published - 12-May-2011|
- VISIBLE ABSORPTION-SPECTROSCOPY, COLLAGEN TRIPLE-HELIX, MOLECULAR-DYNAMICS, CONFORMATIONAL DYNAMICS, SECONDARY STRUCTURE, TRANS-AZOBENZENE, CYCLIC PEPTIDE, AMINO-ACID, SHEET, PROTEINS