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Orientational and dynamical heterogeneity of rhodamine 6G terminally attached to a DNA helix revealed by NMR and single-molecule fluorescence spectroscopy.

Abstract:

The comparison of Förster resonance energy transfer (FRET) efficiencies between two fluorophores covalently attached to a single protein or DNA molecule is an elegant approach for deducing information about their structural and dynamical heterogeneity. For a more detailed structural interpretation of single-molecule FRET assays, information about the positions as well as the dynamics of the dye labels attached to the biomolecule is important. In this work, Rhodamine 6G (2-[3'-(ethylamino)-6'-...

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Publication status:
Published

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Publisher copy:
10.1021/ja0722574

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
Weatherall Insti. of Molecular Medicine
Role:
Author
Journal:
Journal of the American Chemical Society More from this journal
Volume:
129
Issue:
42
Pages:
12746-12755
Publication date:
2007-10-01
DOI:
EISSN:
1520-5126
ISSN:
0002-7863

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