Miki M, Mihashi K
Biophys Chem. 1976 Dec;6(1):101-6. doi: 10.1016/0301-4622(76)80066-x.
The excitation polarization spectrum of epsilon-ADP bound to F-actin shows that two absorption dipoles at 260 nm and 340 nm are oriented in different directions relative to the emission dipole. On the other hand, the linear dichroism of F-actin-epsilon-ADP gives that the dichroic ratio of the bound epsilon-ADP is approximately constant (about-0.5) in the wavelength region form 250 to 350nm. Furthermore, the fluorescence polarization of epsilon-ADP bound to F-actin which is oriented in the field of flow shows that the emission dipole is nearly perpendicular to the long axis of F-actin. From these observations we conclude that the adenine plane of the bound nucleotide is almost perpendicular to the long axis of F-actin.
与F-肌动蛋白结合的ε-ADP的激发偏振光谱表明，在260nm和340nm处的两个吸收偶极子相对于发射偶极子的取向不同。另一方面，F-肌动蛋白-ε-ADP的线性二色性表明，结合的ε-ADP的二色性比率在250至350nm的波长区域内近似恒定（约为-0.5）。此外，在流动场中取向的与F-肌动蛋白结合的ε-ADP的荧光偏振表明，发射偶极子几乎垂直于F-肌动蛋白的长轴。从这些观察结果我们得出结论，结合核苷酸的腺嘌呤平面几乎垂直于F-肌动蛋白的长轴。
