| Literature DB >> 25108686 |
David Arnlund1, Linda C Johansson1, Cecilia Wickstrand1, Anton Barty2, Garth J Williams3, Erik Malmerberg1, Jan Davidsson4, Despina Milathianaki3, Daniel P DePonte5, Robert L Shoeman6, Dingjie Wang7, Daniel James7, Gergely Katona1, Sebastian Westenhoff1, Thomas A White2, Andrew Aquila2, Sadia Bari8, Peter Berntsen1, Mike Bogan9, Tim Brandt van Driel10, R Bruce Doak11, Kasper Skov Kjær12, Matthias Frank13, Raimund Fromme14, Ingo Grotjohann14, Robert Henning15, Mark S Hunter14, Richard A Kirian7, Irina Kosheleva15, Christopher Kupitz14, Mengning Liang2, Andrew V Martin2, Martin Meedom Nielsen10, Marc Messerschmidt5, M Marvin Seibert3, Jennie Sjöhamn1, Francesco Stellato2, Uwe Weierstall7, Nadia A Zatsepin7, John C H Spence7, Petra Fromme14, Ilme Schlichting6, Sébastien Boutet3, Gerrit Groenhof16, Henry N Chapman17, Richard Neutze1.
Abstract
We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions.Entities:
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Year: 2014 PMID： 25108686 PMCID： PMC4149589 DOI： 10.1038/nmeth.3067
Source DB: PubMed Journal: Nat Methods ISSN： 1548-7091 Impact factor: 28.547