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Dynamics of transition dipole moment orientation in representative fluorescent proteins
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SYSNO ASEP 0574393 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Dynamics of transition dipole moment orientation in representative fluorescent proteins Author(s) Khoroshyy, Petro (UOCHB-X) ORCID, RID
Martinez-Seara, Hector (UOCHB-X) RID, ORCID
Myšková, J. (CZ)
Lazar, Josef (UOCHB-X) ORCID, RIDSource Title Physical Chemistry Chemical Physics. - : Royal Society of Chemistry - ISSN 1463-9076
Roč. 25, č. 33 (2023), s. 22117-22123Number of pages 7 s. Language eng - English Country GB - United Kingdom Keywords quantitative analysis ; anisotropy ; FRET OECD category Physical chemistry R&D Projects EF16_019/0000729 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UOCHB-X - RVO:61388963 UT WOS 001044659900001 EID SCOPUS 85168575563 DOI 10.1039/d3cp01242e Annotation Molecules of fluorescent proteins (FPs) exhibit distinct optical directionality. This optical directionality is characterized by transition dipole moments (TDMs), and their orientation with respect to the molecular structures. Although our recent observations of FP crystals allowed us to determine the mean TDM directions with respect to the framework of representative FP molecules, the dynamics of TDM orientations within FP molecules remain to be ascertained. Here we describe the results of our investigations of the dynamics of TDM directions in the fluorescent proteins eGFP, mTurquoise2 and mCherry, through time-resolved fluorescence polarization measurements and microsecond time scale all-atom molecular dynamics (MD) simulations. The investigated FPs exhibit initial fluorescence anisotropies (r(0)) consistent with significant differences in the orientation of the excitation and emission TDMs. However, based on MD data, we largely attribute this observation to rapid (sub-nanosecond) fluorophore motions within the FP molecular framework. Our results allow improved determinations of orientational distributions of FP molecules by polarization microscopy, as well as more accurate interpretations of fluorescence resonance energy transfer (FRET) observations. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2024 Electronic address https://doi.org/10.1039/D3CP01242E
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