Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization

Abstract

Photocaging in combination with X-ray solution scattering allows for the time-resolved study of protein dynamics in solution. This method is versatile and allows for accurate triggering of protein function.

Tracking Ca 2+ ATPase intermediates in real time by x-ray solution scattering

“…The time-resolved x-ray solution scattering (TR-XSS) methodology can be used to characterize subtle structural dynamics in photoactive chemicals (21), protein dimerization (22), and for tracking of conformational changes of soluble proteins (23)(24)(25)(26), as well as membrane proteins in detergent micelles (8,27) and nanodiscs (28). A hybrid approach capable of resolving both local and global structural rearrangements has also been proposed (29).…”

Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme

“…[13][14][15][16][17][18] ). Unfortunately, the number of proteins that undergo specific photochemistry as part of their functional cycle is small, and there is a fundamental need to develop generalized methods that can be used to synchronously excite conformational transitions in any protein molecule and expand the utility of time-resolved structural experiments [19][20][21][22][23][24][25][26][27] .…”

Estimating signal and noise of time-resolved X-ray solution scattering data at synchrotrons and XFELs

“…Fast processes in solutions involving short-lived intermediates are often investigated by time-resolved spectroscopy, but the associated molecular structural changes in general are not direct observables of time-resolved spectroscopy, which relies on the transitions between energy states. In this regard, time-resolved X-ray solution scattering (TRXSS), also known as time-resolved X-ray liquidography (TRXL), has been established as a powerful tool for studying molecular structural dynamics in the liquid solution phase Haldrup et al, 2012Haldrup et al, , 2019Salassa et al, 2010;Kim et al, 2012;Ahn et al, 2018;Biasin et al, 2018;Canton et al, 2015;Kong et al, 2019;Leshchev et al, 2018;Berntsson et al, 2017;Josts et al, 2018;Kim, Ganesan, et al, al., 2009;Christensen et al, 2009;Cammarata et al, 2006Cammarata et al, , 2008Kong et al, 2007;Ihee et al, 2005;Plech et al, 2004). In a typical experiment, an optical laser pulse is used to initiate a reaction and after a time delay an X-ray pulse is sent to probe the reaction progress via X-ray scattering.…”

“…In a typical experiment, an optical laser pulse is used to initiate a reaction and after a time delay an X-ray pulse is sent to probe the reaction progress via X-ray scattering. TRXL has been applied to a wide range of molecules ranging from small molecules such as organometallic compounds (Biasin et al, 2018;Kong et al, 2019;Leshchev et al, 2018;Canton et al, 2015;Haldrup et al, 2012;Salassa et al, 2010;Haldrup et al, 2019;Kong et al, 2007) and hydrocarbons (Ahn et al, 2018;Kim et al, 2012;Ihee et al, 2005;Davidsson et al, 2005) to macromolecules such as proteins (Berntsson et al, 2017;Josts et al, 2018;Kim, Ganesan, et al, 2018;Rimmerman et al, 2017;Arnlund et al, 2014;Kim, Muniyappan, et al, 2016;Malmerberg et al, 2011Malmerberg et al, , 2015Konuma et al, 2011;Westenhoff et al, 2010;Cho et al, 2010;Andersson et al, 2009;Cammarata et al, 2008). Due to the successful applications of TRXL to a wide range of molecules and reactions, applications of TRXL are expected to increase in the future.…”