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    Wyświetlanie 1-6 z 6
    Tytuł:
    Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate
    Autorzy:
    Bertrand, Quentin
    Nogły, Przemysław
    Nass, Karol
    Iwata, So
    Schertler, Gebhard
    Tanaka, Rie
    Standfuss, Jörg
    James, Daniel
    Brünle, Steffen
    Furrer, Antonia
    Weinert, Tobias
    Kepa, Michal
    Kekilli, Demet
    Panneels, Valerie
    Börjesson, Per
    Ortolani, Giorgia
    Skopintsev, Petr
    Tanaka, Tomoyuki
    Huang, Chia-Ying
    Mous, Sandra
    Neutze, Richard
    Tono, Kensuke
    Johnson, Philip J. M.
    Khusainov, Georgii
    Knopp, Gregor
    Owada, Shigeki
    Martiel, Isabelle
    Ozerov, Dmitry
    Milne, Christopher
    Dworkowski, Florian
    Nango, Eriko
    Cirelli, Claudio
    Opis:
    Time-resolved serial crystallography at X-ray Free Electron Lasers offers the opportunity to observe ultrafast photochemical reactions at the atomic level. The technique has yielded exciting molecular insights into various biological processes including light sensing and photochemical energy conversion. However, to achieve sufficient levels of activation within an optically dense crystal, high laser power densities are often used, which has led to an ongoing debate to which extent photodamage may compromise interpretation of the results. Here we compare time-resolved serial crystallographic data of the bacteriorhodopsin K-intermediate collected at laser power densities ranging from 0.04 to 2493 GW/cm2 and follow energy dissipation of the absorbed photons logarithmically from picoseconds to milliseconds. Although the effects of high laser power densities on the overall structure are small, in the upper excitation range we observe significant changes in retinal conformation and increased heating of the functionally critical counterion cluster. We compare light-activation within crystals to that in solution and discuss the impact of the observed changes on bacteriorhodopsin biology.
    Dostawca treści:
    Repozytorium Uniwersytetu Jagiellońskiego
    Artykuł
    Tytuł:
    Ultrafast structural changes direct the first molecular events of vision
    Autorzy:
    Mühle, Jonas
    Kabanova, Victoria
    Tsai, Ching-Ju
    Cirelli, Claudio
    Skopintsev, Petr
    James, Daniel
    Sen, Saumik
    Diethelm, Azeglio D.
    Deupi, Xavier
    Panneels, Valerie
    Martiel, Isabelle
    Iwata, So
    Milne, Christopher J.
    Wach, Anna
    Guixà-González, Ramon
    Kekilli, Demet
    Glover, Hannah
    Knopp, Gregor
    Brünle, Steffen
    Mous, Sandra
    Boutet, Sébastien
    Standfuss, Jörg
    Tanaka, Rie
    Ortolani, Giorgia
    Sarabi, Daniel
    Gotthard, Guillaume
    Joti, Yasumasa
    Johnson, Philip J. M.
    Tono, Kensuke
    Rodrigues, Matthew J.
    Casadei, Cecilia M.
    Båth, Petra
    Furrer, Antonia
    Nogły, Przemysław
    Weinert, Tobias
    Neutze, Richard
    Nango, Eriko
    Varma, Niranjan
    Schertler, Gebhard
    Ma, Pikyee
    Bacellar, Camila
    Nass, Karol
    Gruhl, Thomas
    Lesca, Elena
    Tejero, Oliver
    Dworkowski, Florian
    Ozerov, Dmitry
    Owada, Shigeki
    Pamula, Filip
    Gashi, Dardan
    Opis:
    Vision is initiated by the rhodopsin family of light-sensitive G protein-coupled receptors (GPCRs)1. A photon is absorbed by the 11-cis retinal chromophore of rhodopsin, which isomerizes within 200 femtoseconds to the all-trans conformation2, thereby initiating the cellular signal transduction processes that ultimately lead to vision. However, the intramolecular mechanism by which the photoactivated retinal induces the activation events inside rhodopsin remains experimentally unclear. Here we use ultrafast time-resolved crystallography at room temperature to determine how an isomerized twisted all-trans retinal stores the photon energy that is required to initiate the protein conformational changes associated with the formation of the G protein-binding signalling state. The distorted retinal at a 1-ps time delay after photoactivation has pulled away from half of its numerous interactions with its binding pocket, and the excess of the photon energy is released through an anisotropic protein breathing motion in the direction of the extracellular space. Notably, the very early structural motions in the protein side chains of rhodopsin appear in regions that are involved in later stages of the conserved class A GPCR activation mechanism. Our study sheds light on the earliest stages of vision in vertebrates and points to fundamental aspects of the molecular mechanisms of agonist-mediated GPCR activation.
    Dostawca treści:
    Repozytorium Uniwersytetu Jagiellońskiego
    Artykuł
      Wyświetlanie 1-6 z 6

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