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faculty: "FNWI" and publication year: "2012"
| Authors||D.M. Shcherbakova, M.A. Hink, L. Joosen, Th.W.J. Gadella, V.V. Verkhusha|
|Title||An orange fluorescent protein with a large Stokes shift for single-excitation multicolor FCCS and FRET imaging.|
|Journal||Journal of the American Chemical Society|
|Faculty||Faculty of Science|
|Institute/dept.||FNWI: Swammerdam Institute for Life Sciences (SILS)|
|Abstract||Multicolor imaging based on genetically-encoded fluorescent proteins (FPs) is a powerful approach to study several dynamic processes in a live cell. We report a monomeric orange FP with a large Stokes shift (LSS), called LSSmOrange (excitation/emission at 437/572 nm), which fills up an existing spectral gap between the green-yellow and red LSSFPs. Brightness of LSSmOrange is 5-fold larger than that of the brightest red LSSFP and similar to the green-yellow LSS-FPs. LSSmOrange allows numerous multicolor applications using a single excitation wavelength that was not possible before. Using LSSmOrange we developed a four-color single-laser fluorescence cross-correlation spectroscopy, solely based on FPs. The quadruple cross-correlation combined with photon counting histogram techniques allowed quantitative single-molecule analysis of the particles labeled with four FPs. LSSmOrange was further applied to simultaneously image two Forster resonance energy transfer pairs, one of which is the commonly used CFP-YFP pair, with a single excitation laser. The combination of LSSmOrange-mKate2 and CFP-YFP biosensors enabled imaging of apoptotic activity and calcium fluctuations in real time. The LSSmOrange mutagenesis, low-temperature and isotope effect studies revealed a proton relay for the excited state proton transfer responsible for the LSS phenotype.|
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