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Charge, Color, and Conformation: Spectroscopy on Isomer-Selected Peptide Ions

Abstract : Monitoring the chromism induced by intramolecular hydrogen and charge transfers within proteins as well as the isomerization of both protein and cofactor is essential not only to understand photoactive signaling pathways but also to design targeted opto-switchable proteins. We used a dual-ion mobility drift tube coupled to a tunable picosecond laser to explore the optical and structural properties of a peptide chain bound to a chromophore—a prototype system allowing for a proton transfer coupled to conformational change. With the support of molecular dynamics and DFT calculations, we show how proton transfer between the peptide and its cofactor can dramatically modify the optical properties of the system and demonstrate that these changes can be triggered by collisional activation in the gas phase.
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Contributor : Philippe Dugourd <>
Submitted on : Wednesday, July 20, 2016 - 2:48:45 PM
Last modification on : Tuesday, June 15, 2021 - 2:30:18 PM
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Chang Min Choi, Anne-Laure Simon, Fabien Chirot, Alexander Kulesza, Geoffrey Knight, et al.. Charge, Color, and Conformation: Spectroscopy on Isomer-Selected Peptide Ions. Journal of Physical Chemistry B, American Chemical Society, 2016, 120 (4), pp.709-714. ⟨10.1021/acs.jpcb.5b11919⟩. ⟨hal-01345016⟩



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