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- W156620728 abstract "This chapter focuses on the capability of quantifying protein–protein and other molecular interactions by using fluorescence correlation spectroscopy (FCS). The methods of FCS entail counting experiments, in which the fluorescence signal from within a small optically defined volume serves as a measure of the number of molecules ( N ) within that volume. This number fluctuates as molecules diffuse into and out of the observation volume. There are two key sources of information in the fluctuation signal and each can be used to quantify molecular interactions. First, the duration of the fluctuations is related to the average time individual molecules reside within volume. Second, the amplitude of the fluctuations is determined by the number concentration of independently diffusing molecules occupying the volume. FCS can provide an important complement to Forster resonance energy transfer (FRET) for quantifying molecular interactions. The variations of FCS may often prove to be a superior alternative to FRET." @default.
- W156620728 created "2016-06-24" @default.
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- W156620728 date "2005-01-01" @default.
- W156620728 modified "2023-09-27" @default.
- W156620728 title "Quantifying Molecular Interactions with Fluorescence Correlation Spectroscopy" @default.
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- W156620728 doi "https://doi.org/10.1016/b978-019517720-6.50024-9" @default.
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