Torgerson P M, Morales M F
Proc Natl Acad Sci U S A. 1984 Jun;81(12):3723-7. doi: 10.1073/pnas.81.12.3723.
Fluorescence anisotropy decays were used to quantify the degree of rapid librational motion associated with several fluorescent probes attached to contractile proteins. This information allows an analysis of how far kappa 2, the resonance energy transfer orientation factor, may deviate from the dynamically averaged value of 2/3. Extrema can then be set on R0, the critical transfer distance, and hence on the interprobe distance. These results set maximum ranges on possible distances between several probe pairs used in the mapping of contractile protein structure by resonance energy transfer.
荧光各向异性衰减被用于量化与附着在收缩蛋白上的几种荧光探针相关的快速摆动运动程度。该信息有助于分析κ2（共振能量转移取向因子）可能偏离动态平均值2/3的程度。然后可以在临界转移距离R0上设定极值，进而在探针间距离上设定极值。这些结果为通过共振能量转移绘制收缩蛋白结构时使用的几对探针之间的可能距离设定了最大范围。
