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

Journal article

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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Authors: Neubauer, H; Gaiko, N; Berger, S; Schaffer, J; Eggeling, C

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 129
• Issue: 42
• Pages: 12746-12755
• Publication date: 2007-10-01
• DOI: 10.1021/ja0722574
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Nucleic Acid Conformation; Fluorescent Dyes; Nanotechnology; Photons; Rhodamines; Fluorescence Resonance Energy Transfer; Spectrometry, Fluorescence; Magnetic Resonance Spectroscopy; Models, Chemical; Protein Structure, Secondary; Time Factors; Fluorescence Polarization; Stereoisomerism; Molecular Conformation; DNA