Deciphering Structural Photophysics of Fluorescent Proteins by Kinetic Crystallography.

Abstract : Because they enable labeling of biological samples in a genetically-encoded manner, Fluorescent Proteins (FPs) have revolutionized life sciences. Photo-transformable fluorescent proteins (PTFPs), in particular, recently attracted wide interest, as their fluorescence state can be actively modulated by light, a property central to the emergence of super-resolution microscopy. PTFPs, however, exhibit highly complex photophysical behaviours that are still poorly understood, hampering the rational engineering of variants with improved performances. We show that kinetic crystallography combined with in crystallo optical spectroscopy, modeling approaches and single-molecule measurements constitutes a powerful tool to decipher processes such as photoactivation, photoconversion, photoswitching, photoblinking and photobleaching. Besides potential applications for the design of enhanced PTFPs, these investigations provide fundamental insight into photoactivated protein dynamics.
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Article dans une revue
International Journal of Molecular Sciences, MDPI, 2017, 18 (6), pp.E1187. 〈10.3390/ijms18061187〉
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http://hal.univ-grenoble-alpes.fr/hal-01561575
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Soumis le : jeudi 13 juillet 2017 - 09:35:53
Dernière modification le : jeudi 11 janvier 2018 - 06:15:24

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Dominique Bourgeois. Deciphering Structural Photophysics of Fluorescent Proteins by Kinetic Crystallography.. International Journal of Molecular Sciences, MDPI, 2017, 18 (6), pp.E1187. 〈10.3390/ijms18061187〉. 〈hal-01561575〉

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