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Photoreversible dark state in a tristable green fluorescent protein variant

TitlePhotoreversible dark state in a tristable green fluorescent protein variant
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2003
AuthorsNifosì, R., Ferrari A., Arcangeli Caterina, Tozzinit V., Pellegrini V., and Beltram F.
JournalJournal of Physical Chemistry B
Volume107
Pagination1679-1684
ISSN10895647
KeywordsChromophores, fluorescence, Green fluorescent proteins (GFP), Hydrogen bonds, Optimization, Proteins
Abstract

The reversible photoinduced structural changes of a green fluorescent protein (GFP) mutant and their optical control are reported. A photoreversible optically inactive configuration is demonstrated with the absorption peak at 365 nm, which is consistent with a photoisomerization pathway associated with hydrogen-bond breaking in the chromophore environment. We show that this state is involved in the switching dynamics recently discovered in these molecules and we determine the transition rates of the reversible photoconversion processes. These experiments combine to provide the framework for the implementation and optimization of efficient room-temperature GFP-based all-optical memories that use the fluorescent properties of these proteins.

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URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0037456453&doi=10.1021%2fjp0266852&partnerID=40&md5=0515a0db4d7fb9a65efbd501bf14f6bb
DOI10.1021/jp0266852
Citation KeyNifosì20031679