ArticleThe journal of physical chemistry letters2010
Relaxation Kinetics by Fluorescence Correlation Spectroscopy: Determination of Kinetic Parameters in the Presence of Fluorescent Impurities.
Article in The journal of physical chemistry letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Unraveling multi-state molecular dynamics in single-molecule FRET experiments. II. Quantitative analysis of multi-state kinetic networks.The Journal of chemical physics · 2022Article
- Time-averaged fluorescence intensity analysis in fluorescence fluctuation polarization sensitive experiments.Biomedical optics express · 2013Article
- Dynamics of nucleosome invasion by DNA binding proteins.Journal of molecular biology · 2011Article
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Authors and funding
1 author.
Funding
Abstract
The use of Fluorescence Correlation Spectroscopy (FCS) in combination with Förster Resonance Energy Transfer (FRET) is gaining popularity as a tool to investigate kinetics in equilibrium conditions. The technique is based on the study of fluorescence fluctuations in small numbers of molecules, and is particularly well-suited to investigate conformational dynamics in biopolymers. In practice, its applicability is often hindered by the presence of certain impurities such as partially labeled biomolecules, excess of free fluorophore, or partially dissociated multi-subunit complexes. Here, we show that the simultaneous measurement of the fluctuations in the donor and acceptor intensities allows the determination of the kinetic relaxation time of the reaction in the presence of donor-only particles when cross-talk is negligible, or in cases where all species have the same diffusion coefficient. Theoretical predictions are supported with the results of Monte Carlo simulations, and demonstrate that the applicability of the technique is more general than previously thought.
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