A novel approach to the description of the assembly mechanism of functional biological structures is presented. The approach is based on the identification of fundamental self-assembling processes to which an additional structurization “engineered” by Nature to optimize functions is superimposed. Application of the approach to the structure and contraction of the striated muscle evidences a key role of the residual liquid crystallinity of a constrained structure and the alteration of the compatibility between the thin and thick filaments driven by ionic interactions. ATP hydrolysis boosts the relaxation process. A strong protein scaffold, engineered during the evolutionary process and based on the selective anchoring of coordinated filaments, directs a demixing tendency of the two filaments toward a sliding motion along the fiber axis. The Huxley-Hanson sliding filament hypothesis aimed to explain the contraction-relaxation function of the striated muscle, but does not offer any clue on the overall assembling mechanism of the myofibril.
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