Abstract
Surface structure of myofibrils of rabbit skeletal muscle and their transverse elasticity were studied by atomic force microscopy. Images of myofibrils had a periodic structure characteristic of sarcomeres of skeletal muscle fibers. The transverse elasticity distribution in the sarcomere was determined based on force-distance curves measured at various loci of single myofibrils. The Z-line in rigor myofibrils was the most rigid in all the loci of myofibrils studied under various physiological conditions. The overall transverse elasticity of myofibrils decreased in the order in rigor solution > +AMPPNP solution > relaxing solution. The “apparent” transverse Young's modulus of myofibrils estimated at the overlap region between thin and thick filaments was 84.0 ± 18.1, 37.5 ± 14.0, and 11.5 ± 3.5 kPa in rigor, +AMPPNP, and relaxing solution respectively.
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