放射光セミナー

日時: 2009-12-22 10:00 - 11:00
場所: 4号館2階輪講室1
会議名: 放射光セミナー「Protein structural dynamics visualized by pump-probe time-resolved X-ray crystallography and liquidography」
講演者: Professor Hyotcherl Ihee  (Center for Time-Resolved Diffraction, Department of Chemistry, Graduate)
講演言語: 英語
URL: http:pfwww.kek.jp/pf-seminar/
アブストラクト: The principle, experimental technique, data analysis, and applications of time-resolved X-ray diffraction and scattering to study spatiotemporal reaction dynamics of proteins in single crystals and solutions will be presented. X-ray crystallography, the major structural tool to determine 3D structures of proteins, can be extended to time-resolved X-ray crystallography with a laser-excitation and X-ray-probe scheme, and all the atomic positions in a protein can be tracked during their biological function. However time-resolved crystallography has been limited to a few model systems with reversible photocycles due to the stringent prerequisites such as highly-ordered and radiation-resistant single crystals and crystal packing constraints might hinder biologically relevant motions. These problems can be overcome by applying time-resolved X-ray diffraction directly to protein solutions rather than protein single crystals. To emphasize that structural information can be obtained from the liquid phase, this time-resolved X-ray solution scattering technique is named time-resolved X-ray liquidography in analogy to time-resolved X-ray crystallography where the structural information of reaction intermediates is obtained from the crystalline phase. By providing insights into the structural dynamics of proteins functioning in their natural environment, time-resolved X-ray liquidography complements and extends results obtained with time-resolved pectroscopy and X-ray crystallography. [1] H. Ihee, Acc. Chem. Res. (2009), 42, 356-366. [2] M. Cammarata, M. Levantino, F. Schotte, P. A. Anfinrud, F. Ewald, J. Choi, A. Cupane, M. Wulff, and H. Ihee, Nature Methods (2008), 5, 881-887. [3] H. Ihee, M. Lorenc, T. K. Kim, Q. Y. Kong, M. Cammarata, J. H. Lee, S. Bratos, and M. Wulff, Science (2005), 309, 1223-1227. [4] H. Ihee, S. Rajagopal, V. Srajer, R. Pahl, S. Anderson, M. Schmidt, F. Schotte, P. A. Anfintud, M. Wulff, and K. Moffat, Proc. Natl. Acad. Sci. (2005), 101, 7147-7150.

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