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  Absolute quantum yield measurements of fluorescent proteins using a plasmonic nanocavity

Ruhlandt, D., Andresen, M., Jensen, N. A., Gregor, I., Jakobs, S., Enderlein, J., et al. (2020). Absolute quantum yield measurements of fluorescent proteins using a plasmonic nanocavity. Communications Biology, 3: 627. doi:10.1038/s42003-020-01316-2.

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Ruhlandt, D., Author
Andresen, M.1, Author              
Jensen, N. A.2, Author              
Gregor, I., Author
Jakobs, S.3, Author              
Enderlein, J., Author
Chizhik, A. I., Author
Affiliations:
1Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              
2Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society, ou_578627              
3Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              

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Free keywords: Fluorescence spectroscopy; Single-molecule biophysics
 Abstract: One of the key photophysical properties of fluorescent proteins that is most difficult to measure is the quantum yield. It describes how efficiently a fluorophore converts absorbed light into fluorescence. Its measurement using conventional methods become particularly problematic when it is unknown how many of the proposedly fluorescent molecules of a sample are indeed fluorescent (for example due to incomplete maturation, or the presence of photophysical dark states). Here, we use a plasmonic nanocavity-based method to measure absolute quantum yield values of commonly used fluorescent proteins. The method is calibration-free, does not require knowledge about maturation or potential dark states, and works on minute amounts of sample. The insensitivity of the nanocavity-based method to the presence of non-luminescent species allowed us to measure precisely the quantum yield of photo-switchable proteins in their on-state and to analyze the origin of the residual fluorescence of protein ensembles switched to the dark state.

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Language(s): eng - English
 Dates: 2020-10-30
 Publication Status: Published online
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s42003-020-01316-2
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Title: Communications Biology
Source Genre: Journal
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Pages: 7 Volume / Issue: 3 Sequence Number: 627 Start / End Page: - Identifier: -