Haselgrove J C, Reedy M K
Biophys J. 1978 Dec;24(3):713-28. doi: 10.1016/S0006-3495(78)85415-0.
We have undertaken some computer modeling studies of the cross-bridge observed by Reedy in insect flight muscle so that we investigate the geometric parameters that influence the attachment patterns of cross-bridges to actin filaments. We find that the appearance of double chevrons along an actin filament indicates that the cross-bridges are able to reach 10--14 nm axially, and about 90 degrees around the actin filament. Between three and five actin monomers are therefore available along each turn of one strand of actin helix for labeling by cross-bridges from an adjacent myosin filament. Reedy's flared X of four bridges, which appears rotated 60 degrees at successive levels on the thick filament, depends on the orientation of the actin filaments in the whole lattice as well as on the range of movement in each cross-bridge. Fairly accurate chevrons and flared X groupings can be modeled with a six-stranded myosin surface lattice. The 116-nm long repeat appears in our models as "beating" of the 14.5-nm myosin repeat and the 38.5-nm actin period. Fourier transforms of the labeled actin filaments indicate that the cross-bridges attach to each actin filament on average of 14.5 nm apart. The transform is sensitive to changes in the ease with which the cross-bridge can be distorted in different directions.
我们对里迪在昆虫飞行肌中观察到的横桥进行了一些计算机建模研究,以便研究影响横桥与肌动蛋白丝附着模式的几何参数。我们发现,沿着肌动蛋白丝出现的双V字形表明横桥能够在轴向上延伸10 - 14纳米,并围绕肌动蛋白丝旋转约90度。因此,在肌动蛋白螺旋的每一圈中,沿着一股肌动蛋白丝有三到五个肌动蛋白单体可供相邻肌球蛋白丝的横桥标记。里迪观察到的由四个桥组成的喇叭状X形结构,在粗肌丝上的连续层次上似乎旋转了60度,这取决于整个晶格中肌动蛋白丝的取向以及每个横桥的运动范围。使用六股肌球蛋白表面晶格可以模拟出相当精确的V字形和喇叭状X形结构。在我们的模型中,116纳米长的重复结构表现为14.5纳米的肌球蛋白重复结构和38.5纳米的肌动蛋白周期的“跳动”。标记的肌动蛋白丝的傅里叶变换表明,横桥平均每隔14.5纳米附着在一根肌动蛋白丝上。该变换对横桥在不同方向上变形的难易程度的变化很敏感。