@article{WohlgemuthMitric2016,
  author    = {Wohlgemuth, Matthias and Mitric, Roland},
  title     = {Photochemical Chiral Symmetry Breaking in Alanine},
  series = {Journal of Physical Chemistry A},
  volume    = {45},
  journal   = {Journal of Physical Chemistry A},
  number    = {120},
  doi       = {10.1021/acs.jpca.6b07611},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-158557},
  pages     = {8976-8982},
  year      = {2016},
  abstract  = {We introduce a general theoretical approach for the simulation of photochemical dynamics under the influence of circularly polarized light to explore the possibility of generating enantiomeric enrichment through polarized-light-selective photochemistry. The method is applied to the simulation of the photolysis of alanine, a prototype chiral amino acid. We show that a systematic enantiomeric enrichment can be obtained depending on the helicity of the circularly polarized light that induces the excited-state photochemistry of alanine. By analyzing the patterns of the photoinduced fragmentation of alanine we find an inducible enantiomeric enrichment up to 1.7\%, which is also in good correspondence to the experimental findings. Our method is generally applicable to complex systems and might serve to systematically explore the photochemical origin of homochirality.},
  language  = {en}
}
@article{WohlgemuthMiyazakiTsukadaetal.2017,
  author    = {Wohlgemuth, Matthias and Miyazaki, Mitsuhiko and Tsukada, Kohei and Weiler, Martin and Dopfer, Otto and Fujii, Masaaki and Mitrić, Roland},
  title     = {Deciphering environment effects in peptide bond solvation dynamics by experiment and theory},
  series = {Physical Chemistry Chemical Physics},
  volume    = {19},
  journal   = {Physical Chemistry Chemical Physics},
  number    = {33},
  doi       = {10.1039/C7CP03992A},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-159647},
  pages     = {22564-22572},
  year      = {2017},
  abstract  = {Most proteins work in aqueous solution and the interaction with water strongly affects their structure and function. However, experimentally the motion of a specific single water molecule is difficult to trace by conventional methods, because they average over the heterogeneous solvation structure of bulk water surrounding the protein. Here, we provide a detailed atomistic picture of the water rearrangement dynamics around the -CONH- peptide linkage in the two model systems formanilide and acetanilide, which simply differ by the presence of a methyl group at the peptide linkage. The combination of picosecond pump-probe time-resolved infrared spectroscopy and molecular dynamics simulations demonstrates that the solvation dynamics at the molecular level is strongly influenced by this small structural difference. The effective timescales for solvent migration triggered by ionization are mainly controlled by the efficiency of the kinetic energy redistribution rather than the shape of the potential energy surface. This approach provides a fundamental understanding of protein hydration and may help to design functional molecules in solution with tailored properties.},
  language  = {en}
}