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NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein

Abstract : The availability of fluorescent proteins with distinct phototransformation properties is crucial for a wide range of applications in advanced fluorescence microscopy and biotechnology. To rationally design new variants optimized for specific applications, a detailed understanding of the mechanistic features underlying phototransformation is essential. At present, little is known about the conformational dynamics of fluorescent proteins at physiological temperature and how these dynamics contribute to the observed phototransformation properties. Here, we apply high-resolution NMR spectroscopy in solution combined with in situ sample illumination at different wavelengths to investigate the conformational dynamics of rsFolder, a GFPderived protein that can be reversibly switched between a green fluorescent state and a nonfluorescent state. Our results add a dynamic view to the static structures obtained by x-ray crystallography. Including a custom-tailored NMR toolbox in fluorescent protein research provides new opportunities for investigating the effect of mutations or changes in the environmental conditions on the conformational dynamics of phototransformable fluorescent proteins and their correlation with the observed photochemical and photophysical properties.
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Contributor : Virgile Adam Connect in order to contact the contributor
Submitted on : Tuesday, November 24, 2020 - 4:55:55 PM
Last modification on : Wednesday, November 3, 2021 - 5:36:01 AM
Long-term archiving on: : Thursday, February 25, 2021 - 6:23:53 PM


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Nina Eleni Christou, Isabel Ayala, Karine Giandoreggio-Barranco, Martin Byrdin, Virgile Adam, et al.. NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein. Biophysical Journal, Biophysical Society, 2019, 117 (11), pp.2087-2100. ⟨10.1016/j.bpj.2019.10.035⟩. ⟨hal-02389522⟩



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