This seminar will be presented by Professor Richard Neutze, University of Gothenburg, Sweden.
Time-resolved serial femtosecond crystallography studies at X-ray free electron lasers reveal structural changes in bacteriorhodopsin
X-ray free electron lasers (XFELs) provide a billion-fold jump in the peak X-ray brilliance when compared with synchrotron radiation. One area where XFEL radiation is having an impact is time-resolved structural studies of protein conformational changes.
I will describe how we used time resolved serial femtosecond crystallography at an XFEL to probe light-driven structural changes in bacteriorhodopsin.
Bacteriorhodopsin is a light-driven proton pump which has long been used as a model system in biophysics. The mechanism by which light-driven isomerization of a retinal chromophore is coupled to the transport of protons "up-hill" against a transmembrane proton concentration gradient involves protein structural changes.
Collaborative studies performed at SACLA (an XFEL in Japan) and the LCLS (an XFEL in Stanford, USA) have probed structural changes in bacteriorhodopsin microcrystals on a time-scale from femtoseconds to milliseconds. Structural results from these studies enabled the photoisomerization of retinal to be visualized and a complete picture of structural changes during proton pumping by bacteriorhodopsin to be recovered.
|Date||Tuesday, 11 December 2018|
|Time||10:00am - 11:00am|
|Event Category||Health Sciences|
|Location||Biochemistry Seminar Room 231|