ArticleAnalytical biochemistry1991
Correction for incomplete labeling in the measurement of distance distributions by frequency-domain fluorometry.
Article in Analytical biochemistry, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast Transient Absorption Spectroscopy.Biochemistry · 2016Article
- Myosin-induced movement of alphaalpha, alphabeta, and betabeta smooth muscle tropomyosin on actin observed by multisite FRET.Biophysical journal · 2004Article
- Ca(2+)-induced movement of tropomyosin in skeletal muscle thin filaments observed by multi-site FRET.Biophysical journal · 2002Article
- Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex.Biophysical journal · 2001Article
- Lifetime-based sensing of glucose using energy transfer with a long lifetime donor.Analytical biochemistry · 1997Article
- Time-resolved energy transfer measurements of donor-acceptor distance distributions and intramolecular flexibility of a CCHH zinc finger peptide.Biochemistry · 1993Article
- Distance distributions and anisotropy decays of troponin C and its complex with troponin I.Biochemistry · 1991Article
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5 authors.
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Abstract
Measurements of time-resolved fluorescence are now being used to recover conformational distributions of biological macromolecules. The fluorescence data of the donor are easily corrupted by incomplete labeling of the macromolecules by the acceptor. In the present paper we describe a general procedure to correct for incomplete acceptor labeling in the determination of distance distributions from frequency-domain measurements of the donor fluorescence decay kinetics. The method can also be used to determine the extent of acceptor labeling. Simulated data were used to determine the effect of incomplete labeling on resolution of the distance distribution and the effect on the recovered distributions if one fails to account for incomplete labeling by the acceptor. The expressions and implemented algorithm were verified using known mixtures of donor-control and donor-acceptor pair molecules, which simulated the presence of a donor population lacking the acceptor. Finally, we present data on the distance distributions between two labeled sites in myosin S1 (Cys-697 to Cys-707) where it was not possible to obtain complete labeling of the acceptor site.
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