基于强度范围的定量荧光共振能量转移数据分析以在活细胞核中定位蛋白质分子。
Intensity range based quantitative FRET data analysis to localize protein molecules in live cell nuclei.
作者信息
Chen Ye, Periasamy Ammasi
机构信息
W.M. Keck Center for Cellular Imaging, University of Virginia, Gilmer Hall, Charlottesville, Virginia 22904, USA.
出版信息
J Fluoresc. 2006 Jan;16(1):95-104. doi: 10.1007/s10895-005-0024-1. Epub 2006 Jan 6.
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.
Förster（荧光）共振能量转移（FRET）是一种利用基于强度的显微镜来估计活样本中相互作用蛋白质分子之间距离的理想技术。供体和受体的光谱重叠——这是FRET所必需的——也会产生FRET信号的污染。有许多算法可用于去除这种光谱渗漏（SBT）污染，在本文中，我们比较了两种流行的算法，以估计SBT元素并计算更精确的能量转移效率水平，从而得到更准确的距离估计。
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