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. 2006 Jan;16(1):95-104.
doi: 10.1007/s10895-005-0024-1. Epub 2006 Jan 6.

Intensity range based quantitative FRET data analysis to localize protein molecules in live cell nuclei

Ye Chen  1 , Ammasi Periasamy
Affiliations

Intensity range based quantitative FRET data analysis to localize protein molecules in live cell nuclei

Ye Chen et al. J Fluoresc. 2006 Jan.

Abstract

Förster (fluorescence) resonance energy transfer (FRET) is an ideal technique to estimate the distance between interacting protein molecules in live specimens using intensity-based microscopy. The spectral overlap of donor and acceptor- essential for FRET-also generates a contamination of the FRET signal. There are a number of algorithms available to remove this spectral bleedthrough (SBT) contamination and in this paper we compare two popular algorithms to estimate the SBT element and to calculate a more precise level of energy transfer efficiency, and with that a more accurate distance estimate.

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