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  Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography

Coquelle, N., Sliwa, M., Woodhouse, J., Schirò, G., Adam, V., Aquila, A., et al. (2018). Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography. Nature Chemistry, 10, 31-37. doi:10.1038/nchem.2853.

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Datensatz-Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-FD9C-C Versions-Permalink: http://hdl.handle.net/21.11116/0000-0002-CCE8-3
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NatChemistry_10_2017_31.pdf (beliebiger Volltext), 6MB
 
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https://www.nature.com/articles/nchem.2853.pdf (beliebiger Volltext)
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https://doi.org/10.1038/nchem.2853 (beliebiger Volltext)
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 Urheber:
Coquelle, Nicolas, Autor
Sliwa, Michel, Autor
Woodhouse, Joyce, Autor
Schirò, Giorgio, Autor
Adam, Virgile, Autor
Aquila, Andrew, Autor
Barends, Thomas R. M.1, Autor              
Boutet, Sébastien, Autor
Byrdin, Martin, Autor
Carbajo, Sergio, Autor
la Mora, Eugenio De, Autor
Doak, R. Bruce1, Autor              
Feliks, Mikolaj, Autor
Fieschi, Franck, Autor
Foucar, Lutz1, Autor              
Guillon, Virginia, Autor
Hilpert, Mario1, Autor              
Hunter, Mark S., Autor
Jakobs, Stefan, Autor
Koglin, Jason E., Autor
Kovácsová, Gabriela1, Autor              Lane, Thomas J., AutorLévy, Bernard, AutorLiang, Mengning, AutorNass, Karol1, Autor              Ridard, Jacqueline, AutorRobinson, Joseph S., AutorRoome, Christopher M.1, Autor              Ruckebusch, Cyril, AutorSeaberg, Matthew, AutorThepaut, Michel, AutorCammarata, Marco, AutorDemachy, Isabelle, AutorField, Martin, AutorShoeman, Robert L.1, Autor              Bourgeois, Dominique, AutorColletier, Jacques-Philippe, AutorSchlichting, Ilme1, Autor              Weik, Martin, Autor mehr..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Zusammenfassung: Chromophores absorb light in photosensitive proteins and thereby initiate fundamental biological processes such as photosynthesis, vision and biofluorescence. An important goal in their understanding is the provision of detailed structural descriptions of the ultrafast photochemical events that they undergo, in particular of the excited states that connect chemistry to biological function. Here we report on the structures of two excited states in the reversibly photoswitchable fluorescent protein rsEGFP2. We populated the states through femtosecond illumination of rsEGFP2 in its non-fluorescent off state and observed their build-up (within less than one picosecond) and decay (on the several picosecond timescale). Using an X-ray free-electron laser, we performed picosecond time-resolved crystallography and show that the hydroxybenzylidene imidazolinone chromophore in one of the excited states assumes a near-canonical twisted configuration halfway between the trans and cis isomers. This is in line with excited-state quantum mechanics/molecular mechanics and classical molecular dynamics simulations. Our new understanding of the structure around the twisted chromophore enabled the design of a mutant that displays a twofold increase in its off-to-on photoswitching quantum yield.

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Sprache(n): eng - Englisch
 Datum: 2016-03-062017-07-272017-09-112018-01-01
 Publikationsstatus: Im Druck veröffentlicht
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1038/nchem.2853
 Art des Abschluß: -

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Titel: Nature Chemistry
  Kurztitel : Nat. Chem.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: London, UK : Nature Publishing Group
Seiten: - Band / Heft: 10 Artikelnummer: - Start- / Endseite: 31 - 37 Identifikator: ISSN: 1755-4330
CoNE: /journals/resource/1755-4330