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Unraveling Ultrafast Photoinduced Proton Transfer Dynamics in a Fluorescent Protein Biosensor for Ca²⁺ Imaging Public Deposited

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  • Imaging Ca²⁺ dynamics in living systems holds great potential to advance neuroscience and cellular biology. G-GECO1.1 is an intensiometric fluorescent protein Ca²⁺-biosensor with a Thr-Tyr-Gly chromophore. The protonated chromophore emits green upon photoexcitation via excited-state proton transfer (ESPT). Upon Ca²⁺ binding, a significant population of the chromophores becomes deprotonated. It remains elusive how the chromophore structurally evolves prior to and during ESPT, and how it is affected by Ca²⁺. We use femtosecond stimulated Raman spectroscopy to dissect ESPT in both the Ca²⁺-free and bound states. The protein chromophores exhibit a sub-200 fs vibrational frequency shift due to coherent small-scale proton motions. After wavepackets move out of the Franck-Condon region, ESPT gets faster in the Ca²⁺-bound protein, indicative of the formation of a more hydrophilic environment. These results reveal the governing structure-function relationship of Ca²⁺-sensing protein biosensors.
  • This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by John Wiley & Sons, Inc., and can be found at: http://onlinelibrary.wiley.com/journal/10.1002/%28ISSN%291521-3765
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  • Tang, L., Liu, W., Wang, Y., Zhao, Y., Oscar, B. G., Campbell, R. E., & Fang, C. (2015). Unraveling ultrafast photoinduced proton transfer dynamics in a fluorescent protein biosensor for Ca²⁺ imaging. Chemistry-A European Journal, 21(17), 6481-6490. doi:10.1002/chem.201500491
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  • 21
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  • 17
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  • This work is supported by the Oregon State University (OSU) Faculty Research Start-up Grant and General Research Fund (to C.F.), Natural Sciences and Engineering Research Council of Canada and Canadian Institutes of Health Research (to R.E.C.), and a University of Alberta fellowship and an Alberta Innovates scholarship (to Y.Z.). We appreciate the 2014 OSU chemistry departmental summer research fellowships including the David P. Shoemaker Memorial Research Project (to B.G.O.) and the Dorothy and Ramon Barnes Graduate Fellowship (to Y.W.). We also acknowledge the recent NSF CAREER Award (CHE-1455353) to C.F.
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  • description.provenance : Approved for entry into archive by Deanne Bruner(deanne.bruner@oregonstate.edu) on 2015-10-23T18:27:44Z (GMT) No. of bitstreams: 1 FangChongChemistryUnraveling UltrafastPhotoinducedProtonTransferDynamics.pdf: 2852525 bytes, checksum: 3efe31ffafdb2cec59662699f18511c3 (MD5)
  • description.provenance : Made available in DSpace on 2015-10-23T18:27:44Z (GMT). No. of bitstreams: 1 FangChongChemistryUnraveling UltrafastPhotoinducedProtonTransferDynamics.pdf: 2852525 bytes, checksum: 3efe31ffafdb2cec59662699f18511c3 (MD5) Previous issue date: 2015-04-20
  • description.provenance : Submitted by Deanne Bruner (deanne.bruner@oregonstate.edu) on 2015-10-23T18:26:11Z No. of bitstreams: 1 FangChongChemistryUnraveling UltrafastPhotoinducedProtonTransferDynamics.pdf: 2852525 bytes, checksum: 3efe31ffafdb2cec59662699f18511c3 (MD5)

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