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Myosin-II's rod-like tail drives filament assembly with a head arrangementthat should generate equal and opposite contractile forces on actin--if oneassumes that the filament is a symmetric bipole. Self-assembled myosinfilaments are shown here to be asymmetric in physiological buffer based oncross-correlated images from both atomic force microscopy (AFM) and totalinternal reflection fluorescence (TIRF). Quantitative cross-correlation ofthese orthogonal methods produces structural information unavailable to eithermethod alone in showing that fluorescence intensity along the filament lengthis proportional to height. This implies that myosin heads form a shell aroundthe filament axis, consistent with F-actin binding. A motor density of ~50 -100 heads/micron is further estimated but with an average of 32% more motors onone half of any given filament compared to the other, regardless of length. Apurely entropic pyramidal lattice model is developed that qualitativelycaptures this lack of length dependence and the distribution of filamentasymmetries. Such strongly asymmetric bipoles are likely to produce animbalanced contractile force in cells and in actin-myosin gels, and therebycontribute to motility as well as cytoskeletal tension.

Cross-correlated TIRF/AFM shows Self-assembled Synthetic Myosin Filaments are Asymmetric - Implications for Motile Filaments