McLachlan A D, Karn J
Nature. 1982 Sep 16;299(5880):226-31. doi: 10.1038/299226a0.
The amino acid sequence of the rod portion of nematode myosin, deduced for the sequence of the unc-54 heavy chain gene of Caenorhabditis elegans, is highly repetitive and has the characteristics of an alpha-helical coiled coil. The molecular surface contains alternate clusters of positive and negative charge. Interactions between charge clusters on adjacent molecules could account for the observed spacing of the myosin cross-bridges in muscle. Calculations also suggest that the N-terminal third of the rod is only loosely associated with the thick filament backbone. Bending of the rod near the end of this region could allow the N-terminal section to act as a hinged arm during muscle contraction.
根据秀丽隐杆线虫unc-54重链基因序列推导出来的线虫肌球蛋白杆状部分的氨基酸序列具有高度重复性，且具有α-螺旋卷曲螺旋的特征。分子表面包含正负电荷交替的簇。相邻分子上电荷簇之间的相互作用可以解释在肌肉中观察到的肌球蛋白横桥间距。计算还表明，杆状部分的N端三分之一仅与粗肌丝主干松散相连。在该区域末端附近杆状部分的弯曲可使N端部分在肌肉收缩过程中充当铰链臂。
