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og-title: Dynamic tuning of FRET in a green fluorescent protein biosensor
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article:published_time: 2019-08-01
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dc:title: Dynamic tuning of FRET in a green fluorescent protein biosensor | Science Advances
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DC.Identifier: 10.1126/sciadv.aaw4988
DC.Rights: Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).. This is an open-access article distributed under the terms of the Creative Commons Attribution license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
citation_author: Pablo Trigo-Mourino
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citation_title: Dynamic tuning of FRET in a green fluorescent protein biosensor
citation_author_institution: Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
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title: Dynamic tuning of FRET in a green fluorescent protein biosensor | Science Advances
twitter:image: https://advances.sciencemag.org/sites/default/files/highwire/advances/5/8.cover-source.gif
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DC.Description: Förster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with
Förster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with -dependent paramagnetic nuclear magnetic resonance at 900 MHz and 1.1 GHz. These structural data provide the unprecedented opportunity to calculate FRET from the x-ray structure and to compare it to experimental data in solution. We find that interdomain dynamics limits the FRET effect and show that a rigidification of the sensor further enhances FRET.
DC.Title: Dynamic tuning of FRET in a green fluorescent protein biosensor issue_cover_image: https://advances.sciencemag.org/sites/default/files/highwire/advances/5/8.cover-source.gif citation_firstpage: eaaw4988 X-UA-Compatible: IE=edge,chrome=1 MobileOptimized: width citation_funding_source: citation_funder=Alexander von Humboldt-Stiftung;citation_funder_id=http://dx.doi.org/10.13039/100005156; HW.pisa: advances;5/8/eaaw4988 viewport: width=device-width, initial-scale=1 DC.Language: en twitter:description: Förster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with