Abstract's Details

Watching Proteins Function with Picosecond (today) and Femtosecond (tomorrow) Time-resolved Laue Crystallography
Abstract ID	W:LED-05
Presenter	Philip Anfinrud
Presentation Type	Laser Excited Dynamics
Full Author List	P. A. Anfinrud (1)
Affiliations	(1) National Institutes of Health/NIDDK
Category	Bio/Life Sciences
Abstract	In 1996, Moffat and coworkers introduced the method of nanosecond time-resolved Laue crystallography [1]. Their pioneering work demonstrated to the world that the dream of following correlated structure changes in molecules as complex as proteins could be realized. Since that time, we have developed methods suitable for probing structural changes in proteins on the 100-ps timescale with near-atomic spatial resolution [2,3]. Because structural changes in proteins can propagate at velocities up to the speed of sound, observing these functionally-important motions in real time will require sub-ps time resolution. The LCLS promises to deliver X-ray pulses of a duration and intensity that could make this dream a reality. Experimental approaches suitable for triggering and visualizing structural changes in proteins on ultrafast time scales will be discussed.
Footnotes	[1] Srajer, V. et al., Science 274, 1726 (1996) [2] - F. Schotte, M. Lim, T.A. Jackson, A.V. Smirnov, J. Soman, J.S. Olson, G.N. Phillips, Jr., M. Wulff, and P.A. Anfinrud, Science, 300, 1944, (2003) [3] - F. Schotte, J. Soman, J.S. Olson, M. Wulff, and P.A. Anfinrud, J. Struct. Biol. 147, 235, (2004)
Funding Acknowledgement	This research was supported by the Intramural Research Program of the NIH, NIDDK.