Blyakhman F, Tourovskaya A, Pollack G H
Department of Bioengineering, University of Washington, Seattle Washington 98195, USA.
Biophys J. 2001 Aug;81(2):1093-100. doi: 10.1016/S0006-3495(01)75766-9.
We carried out experiments on single isolated myofibrils in which thin filaments had been functionally removed, leaving the connecting (titin) filaments as the sole agent taking up the length change. With technical advances that gave sub-nanometer detectability we examined the time course of single sarcomere-length change when the myofibril was ramp-released or ramp-stretched by a motor. The sarcomere-length change was stepwise. Step sizes followed a consistent pattern: the smallest was approximately 2.3 nm, and others were integer multiples of that value. The approximately 2.3-nm step quantum is the smallest consistent biomechanical event ever demonstrated. Although the length change must involve the connecting filament, the size of the quantum is an order of magnitude smaller than anticipated from folding of Ig- or fibronectin-like domains, implying either that folding occurs in sub-domain units or that other mechanisms are involved.
我们对单个分离的肌原纤维进行了实验,其中细肌丝已被功能性去除,仅留下连接(肌联蛋白)丝作为承担长度变化的唯一因素。随着检测精度达到亚纳米级的技术进步,我们研究了通过电机对肌原纤维进行斜坡式释放或斜坡式拉伸时单个肌节长度变化的时间进程。肌节长度变化是逐步的。步长遵循一致的模式:最小步长约为2.3纳米,其他步长是该值的整数倍。约2.3纳米的步长量子是有史以来证明的最小的一致生物力学事件。尽管长度变化必然涉及连接丝,但该量子的大小比由免疫球蛋白或纤连蛋白样结构域折叠所预期的小一个数量级,这意味着要么折叠发生在亚结构域单元中,要么涉及其他机制。