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Fluorescent proteins for single‐molecule fluorescence applications
Author(s) -
Seefeldt Britta,
Kasper Robert,
Seidel Thorsten,
Tinnefeld Philip,
Dietz KarlJosef,
Heilemann Mike,
Sauer Markus
Publication year - 2008
Publication title -
journal of biophotonics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 66
eISSN - 1864-0648
pISSN - 1864-063X
DOI - 10.1002/jbio.200710024
Subject(s) - mcherry , fluorescence , fluorescence in the life sciences , förster resonance energy transfer , fluorophore , green fluorescent protein , biophysics , chemistry , bimolecular fluorescence complementation , fluorescence microscope , single molecule experiment , fluorescence lifetime imaging microscopy , molecule , biomolecule , quantum yield , biology , biochemistry , physics , optics , organic chemistry , gene
We present single‐molecule fluorescence data of fluorescent proteins GFP, YFP, DsRed, and mCherry, a new derivative of DsRed. Ensemble and single‐molecule fluorescence experiments proved mCherry as an ideally suited fluorophore for single‐molecule applications, demonstrated by high photostability and rare fluorescence‐intensity fluctuations. Although mCherry exhibits the lowest fluorescence quantum yield among the fluorescent proteins investigated, its superior photophysical characteristics suggest mCherry as an ideal alternative in single‐molecule fluorescence experiments. Due to its spectral characteristics and short fluorescence lifetime of 1.46 ns, mCherry complements other existing fluorescent proteins and is recommended for tracking and localization of target molecules with high accuracy, fluorescence resonance energy transfer (FRET), fluorescence lifetime imaging microscopy (FLIM), or multicolor applications. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)