Intensity range based quantitative FRET data analysis to localize protein molecules in live cell nuclei
Intensity range based quantitative FRET data analysis to localize protein molecules in live cell nuclei
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DOI：
10.1007/s10895-005-0024-1
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发表时间：
2006-01-01
影响因子：
2.7
通讯作者：
Periasamy, A
中科院分区：
文献类型：
--
作者：
Chen, Y;Periasamy, A
福斯特（荧光）共振能量转移（FRET）是一种理想的技术来估计之间的距离相互作用的蛋白质分子在活标本使用强度为基础的显微镜。供体和受体的光谱重叠-FRET所必需的-也产生FRET信号的污染。有许多算法可用于消除这种光谱渗漏（SBT）污染，在本文中，我们比较了两种流行的算法来估计SBT元素，并计算更精确的能量传输效率水平，以及更准确的距离估计。
Forster (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.