Labeling proteins for single-molecule FRET.
Copyright policy )Labeling proteins for single-molecule FRET.
Single-molecule (sm) fluorescence detection is a powerful method for studying biological events without time and population averaging. Förster (fluorescence) resonance energy transfer (FRET) is a spectroscopic technique for measuring distances in the 30-80 Å range in which excitation energy of a donor molecule is transferred to an acceptor via interaction between two induced dipoles. A variant of smFRET is based on total internal reflection (TIR) microscopy. This protocol describes the labeling of protein for smFRET with TIR microscopy. It is based on a labeling procedure for E. coli Rep helicase. A different assay (e.g., different chemical conditions) may be required for other proteins.
Staining and Labeling, Escherichia coli Proteins, DNA Helicases, Escherichia coli, Fluorescence Resonance Energy Transfer, Proteins, Fluorescence, Fluorescent Dyes
Staining and Labeling, Escherichia coli Proteins, DNA Helicases, Escherichia coli, Fluorescence Resonance Energy Transfer, Proteins, Fluorescence, Fluorescent Dyes
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