Imperial College London
Portrait Picture

ProfessorJaspervan Thor

Faculty of Natural Sciences, Department of Life Sciences

Professor of Molecular Biophysics
 
 
 
//

Contact

 

+44 (0)20 7594 5071j.vanthor Website

 
 
//

Location

 

703Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Pande:2016:10.1126/science.aad5081,
author = {Pande, K and Hutchison, CDM and Groenhof, G and Aquila, A and Robinson, JS and Tenboer, J and Basu, S and Boutet, S and DePonte, DP and Liang, M and White, TA and Zatsepin, NA and Yefanov, O and Morozov, D and Oberthuer, D and Gati, C and Subramanian, G and James, D and Zhao, Y and Koralek, J and Brayshaw, J and Kupitz, C and Conrad, C and Roy-Chowdhury, S and Coe, JD and Metz, M and Xavier, PL and Grant, TD and Koglin, JE and Ketawala, G and Fromme, R and rajer, V and Henning, R and Spence, JCH and Ourmazd, A and Schwander, P and Weierstall, U and Frank, M and Fromme, P and Barty, A and Chapman, HN and Moffat, K and van, Thor JJ and Schmidt, M},
doi = {10.1126/science.aad5081},
journal = {Science},
pages = {725--729},
title = {Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein},
url = {http://dx.doi.org/10.1126/science.aad5081},
volume = {352},
year = {2016}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein.Science, this issue p. 725A variety of organisms have evolved mechanisms to detect and respond to light, in which the response is mediated by protein structural changes after photon absorption. The initial step is often the photoisomerization of a conjugated chromophore. Isomerization occurs on ultrafast time scales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans-to-cis isomerization of the chromophore in photoactive yellow protein. Femtosecond hard x-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on photoactive yellow protein microcrystals over a time range from 100 femtoseconds to 3 picoseconds to determine the structural dynamics of the photoisomerization reaction.
AU  - Pande,K
AU  - Hutchison,CDM
AU  - Groenhof,G
AU  - Aquila,A
AU  - Robinson,JS
AU  - Tenboer,J
AU  - Basu,S
AU  - Boutet,S
AU  - DePonte,DP
AU  - Liang,M
AU  - White,TA
AU  - Zatsepin,NA
AU  - Yefanov,O
AU  - Morozov,D
AU  - Oberthuer,D
AU  - Gati,C
AU  - Subramanian,G
AU  - James,D
AU  - Zhao,Y
AU  - Koralek,J
AU  - Brayshaw,J
AU  - Kupitz,C
AU  - Conrad,C
AU  - Roy-Chowdhury,S
AU  - Coe,JD
AU  - Metz,M
AU  - Xavier,PL
AU  - Grant,TD
AU  - Koglin,JE
AU  - Ketawala,G
AU  - Fromme,R
AU  - rajer,V
AU  - Henning,R
AU  - Spence,JCH
AU  - Ourmazd,A
AU  - Schwander,P
AU  - Weierstall,U
AU  - Frank,M
AU  - Fromme,P
AU  - Barty,A
AU  - Chapman,HN
AU  - Moffat,K
AU  - van,Thor JJ
AU  - Schmidt,M
DO  - 10.1126/science.aad5081
EP  - 729
PY  - 2016///
SN  - 1095-9203
SP  - 725
TI  - Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein
T2  - Science
UR  - http://dx.doi.org/10.1126/science.aad5081
UR  - https://science.sciencemag.org/content/352/6286/725/
UR  - http://hdl.handle.net/10044/1/33229
VL  - 352
ER  -
Download