International Research Journals

Short Communication - International Research Journal of Biochemistry and Bioinformatics ( 2021) Volume 11, Issue 3

Richard Neutze*, Eriko Nango, Tomoyuki Tanaka, Takanori Nakane, So Iwata, Antoine Royant, Jorg Standfuss, Przemyslaw Nogly and Cecilia Wickstrand
Public university in Gothenburg, Sweden
*Corresponding Author:
Richard Neutze, Public university in Gothenburg, Sweden,

Published: 28-Jun-2021


X-ray free electron lasers (XFEL) provide a billionfold jump in the peak X-ray brilliance when compared with synchrotron radiation. One area where XFEL radiation has an impact is time-resolved structural studies of protein conformational changes. This presentation 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 †œup-hill†• against a transmembrane proton concentration gradient involves protein structural changes.

Collaborative studies performed at SACLA (the Japanese XFEL) have probed structural changes in microcrystals on a time-scale from nanoseconds to milliseconds.

Structural results from these studies enabled a complete picture of structural changes occurring during proton pumping by bacteriorhodopsin to be recovered