title: Modeling rigor cross-bridge patterns in muscle I. Initial studies of the rigor lattice of insect flight muscle.
abstract: 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.
mesh_terms: D000199:Actins / Q000502:physiology; D000818:Animals; D003201:Computers; D005426:Flight, Animal; D005583:Fourier Analysis; D007313:Insecta / Q000502:physiology; D008954:Models, Biological; D009119:Muscle Contraction; D009210:Myofibrils / Q000648:ultrastructure*; D009218:Myosins / Q000502:physiology
chemical_list: D000199:Actins; D009218:Myosins