Dokument-ID Dokumenttyp Verfasser/Autoren Herausgeber Haupttitel Abstract Auflage Verlagsort Verlag Erscheinungsjahr Seitenzahl Schriftenreihe Titel Schriftenreihe Bandzahl ISBN Quelle der Hochschulschrift Konferenzname Quelle:Titel Quelle:Jahrgang Quelle:Heftnummer Quelle:Erste Seite Quelle:Letzte Seite URN DOI Abteilungen OPUS4-15964 Wissenschaftlicher Artikel Wohlgemuth, Matthias; Miyazaki, Mitsuhiko; Tsukada, Kohei; Weiler, Martin; Dopfer, Otto; Fujii, Masaaki; Mitrić, Roland Deciphering environment effects in peptide bond solvation dynamics by experiment and theory 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. 2017 22564-22572 Physical Chemistry Chemical Physics 19 33 urn:nbn:de:bvb:20-opus-159647 10.1039/C7CP03992A Institut für Physikalische und Theoretische Chemie OPUS4-15948 unpublished Wohlgemuth, Matthias; Miyazaki, Mitsuhiko; Tsukada, Kohei; Weiler, Martin; Dopfer, Otto; Fujii, Masaaki; Mitrić, Roland Deciphering environment effects in peptide bond solvation dynamics by experiment and theory 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. 2017 Physical Chemistry Chemical Physics urn:nbn:de:bvb:20-opus-159483 10.1039/C7CP03992A Fakultät für Chemie und Pharmazie