Barden J A
Biochem Int. 1985 Oct;11(4):583-9.
Modification of Tyr 69 with the chromophore dansyl chloride was found to completely block exchange of the bound ATP on actin. No significant conformational change was detected in the actin after labelling thus indicating that the dansyl chloride is close to and probably sterically blocks the ATP site. The distance separating dansyl chloride attached to Tyr 69 and IAEDANS attached to Cys 374 on actin was found using fluorescence energy transfer to be 3.9 nm. This result is consistent with the known distance between the ATP site and Cys 374.
发现用发色团丹磺酰氯修饰69位酪氨酸可完全阻断肌动蛋白上结合的ATP的交换。标记后未检测到肌动蛋白有明显的构象变化，因此表明丹磺酰氯靠近并可能在空间上阻断了ATP位点。利用荧光能量转移发现，附着在肌动蛋白69位酪氨酸上的丹磺酰氯与附着在374位半胱氨酸上的碘乙酰胺基荧光素之间的距离为3.9纳米。这一结果与ATP位点和374位半胱氨酸之间的已知距离一致。
