ArticleBiophysical journal2011
Rotational diffusion of the α(2a) adrenergic receptor revealed by FlAsH labeling in living cells.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Protein Crowding and Cholesterol Increase Cell Membrane Viscosity in a Temperature Dependent Manner.Journal of chemical theory and computation · 2023Article
- Unraveling the hidden temporal range of fast βCommunications biology · 2022Article
- Strategies for Site-Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags.Chembiochem : a European journal of chemical biology · 2021Review
- Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic TBiophysical journal · 2018Article
- Characterization of Fluorescein Arsenical Hairpin (FlAsH) as a Probe for Single-Molecule Fluorescence Spectroscopy.Scientific reports · 2017Article
- Conformational Profiling of the AT1 Angiotensin II Receptor Reflects Biased Agonism, G Protein Coupling, and Cellular Context.The Journal of biological chemistry · 2017Article
- Rotamer-Restricted Fluorogenicity of the Bis-Arsenical ReAsH.Journal of the American Chemical Society · 2016Article
- Time-resolved FRET reports FGFR1 dimerization and formation of a complex with its effector PLCγ1.Advances in biological regulation · 2016Article
- H-Ras forms dimers on membrane surfaces via a protein-protein interface.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Surveying protein structure and function using bis-arsenical small molecules.Accounts of chemical research · 2011Article
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5 authors.
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Abstract
The fluorescein arsenical hairpin binder (FlAsH) shows much promise to determine the relative orientations of protein regions and structures even in living cells and in the plasma membrane. In this study, we characterized FlAsH's photophysical properties by steady-state anisotropy and time-resolved single photon counting for further applications with G-protein coupled receptors. We find that FlAsH has a relatively high initial anisotropy of 0.31 ± 0.01 and a three-component fluorescence lifetime with an average of 4.1 ± 0.1 ns. We characterized the FlAsH fluorophore orientation in the α(2A) adrenergic receptor revealing rigid orientations of FlAsH in the membrane plane for rotational correlation times of ∼50 ns in living cells. To elucidate the fluorophore-membrane orientation and rotational correlation time, an anisotropy treatment similar to that of another researcher (Axelrod, D. 1979. Biophys. J. 26:557-573) was developed. The rotational correlation times were observed to increase by up to 16 ns after agonist addition. The rotational correlation time also allowed for a comparison to the theoretical relationship between translational and rotational diffusion (originally proposed by Saffman, P. G., and M. Delbrück. 1975. Proc. Natl. Acad. Sci. USA. 72:3111-3113) and revealed a discrepancy of a factor between 10 and 100.
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