Bivin D B, Stone D B, Schneider D K, Mendelson R A
Cardiovascular Research Institute, University of California, San Francisco 94143.
Biophys J. 1991 Apr;59(4):880-8. doi: 10.1016/S0006-3495(91)82300-1.
The cross-helix separation of Tm molecules in acto-tropomyosin has been determined using neutron scattering. Deuterated Dictyostelium discoideum actin was density matched in a 93% D2O buffer so that effectively only the protonated tropomyosin was "visible" to neutrons. Analysis of the solution scattering pattern in the region of the first oscillation yielded a value for the cross-helix separation of 7.9 +/- 0.3 nm. The implications of this value for the mechanism of the regulation of muscle contraction are discussed in light of recent results by others.
利用中子散射测定了肌动蛋白-原肌球蛋白中Tm分子的跨螺旋间距。将氘代盘基网柄菌肌动蛋白在93% D2O缓冲液中进行密度匹配，这样实际上只有质子化的原肌球蛋白能被中子“看到”。对第一次振荡区域的溶液散射图案进行分析，得出跨螺旋间距的值为7.9 +/- 0.3纳米。根据其他人最近的研究结果，讨论了该值对肌肉收缩调节机制的影响。
