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Regensburg 2013 – scientific programme

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BP: Fachverband Biologische Physik

BP 14: Biomaterials and Biopolymers I (joint with CPP)

BP 14.7: Talk

Tuesday, March 12, 2013, 11:30–11:45, H34

Probing the electronic structure of Proline in aqueous solution by soft RIXS — •Frank Meyer1, Andreas Benkert1,2,8, Sankaranarayanan Nagarajan3, Regan Wilks4, Marcus Bär4, Wanli Yang5, Michael Zharnikov3, Clemens Heske2,6,7, Lothar Weinhardt2,6,7, and Friedrich Reinert1,81Exp. Phys. VII, Universität Würzburg — 2Inst. for Photon Science, KIT — 3Angew. Phys. Chemie, Universität Heidelberg — 4Solar Energy Research, HZB — 5ALS, Lawrence Berkeley National Laboratory — 6Dept. of Chemistry, University of Nevada, Las Vegas — 7ANKA Synchrotron Radiation Facility, KIT — 8Gemeinschaftslabor für Nanoanalytik, KIT

Amino acids are organic molecules that are highly relevant for many biological macro-molecules. Defining their function, the electronic structure of these molecules and, in particular, the interaction with biologically relevant solvents is of fundamental interest. In contrast to the majority of amino acids in which the functional groups (carboxyl, amino, side chain) are connected via one carbon atom, in proline the amino group and the side chain are connected in a heterocyclic compound, forming a pyrrolidine ring. We present resonant inelastic soft x-ray scattering (RIXS) maps of proline in aqueous solution at different pH values. Upon protonation and deprotonation, strong changes in the maps are observed. The results will be compared with RIXS data of solid state and gas phase proline, as well as other amino acids (i.e., glycine, cysteine). We find a distinctly different electronic structure than that observed for glycine and cysteine, as well as a significantly influence of the water environment.

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