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Journal Article

Absolute quantum yield measurements of fluorescent proteins using a plasmonic nanocavity

MPS-Authors
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Andresen,  M.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Jensen,  N. A.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

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Jakobs,  S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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3310714.pdf
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Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0008-4C7B-A
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.