Shining a light on protein dynamics says Journal of the American Chemical Society
15 Nov 2013



The CLFs recently developed TRMPS (time-resolved multiple probe spectroscopy) system has been used to study the underlying structural dynamics of the protein domain responsible for organisms that move towards a source of light.



CLF's Greg Greetham, co-author, aligning Ultra's IR beamlines
A group led by Peter Tonge (Stony Brook University, US) andStephen Meech (University of East Anglia, UK) have used Ultra (link opens in a new window)’s advancedpump-probe system to study the structural dynamics of the blue light sensing BLUFdomain found in many photoactive flavoproteins. The newly installed TRMPS (time-resolved multiple probe spectroscopy) system wasemployed to see "proteins in action" and enabled protein response to light stimulation to be explored on avast timescale, covering 100 fs up to 1 ms. A blue 100 fs pump pulse was used in combination with an ultra-short (50fs) infra-red probe pulse with a variety of techniques engaged to achieve thedesired temporal offsets.

The publishedwork (link opens in a new window)reveals the different vibration modes of the protein over the multipletimescales explored, showing how the response of the protein structure cascadesdown to areas remote to the activation area. Most interesting however was theirdiscovery that the relaxation pathway is short-circuited for mutant versions,suppressing the changes which occur far away from the stimulated region whileaccelerating dynamics close to it.

Journal of the American Chemical Society (JACS) has given aspecial mention to this work, describing it as ‘shining a light on proteindynamics’ and was highlighted in the JACS Spotlights feature.


Related article:

CLF science featured on cover of Physical Chemistry Chemical Physics (link opens in a new window)



Contact: Springate, Emma (STFC,RAL,CLF)