We compare steps observed during the fibrillogenesis of myofibrils with the sequence of steps predictable by a recent analysis of the structurization and functioning of striated muscles. The predicted assembly steps are based solely on fundamental equilibrium processes, particularly supramolecular interactions and liquid crystalline alignment of the rigid thick and thin filaments hosted within the sarcomer. Satisfactory agreement is obtained between several of the observed and the predicted fibrillogenesis steps. In several cases, however, the actual steps appear to be more complex than expected, evidencing the occurrence of transport and kinetic pathways that may assist the attainment of the equilibrium structure. The memory of the order of a precursor mesophase is imprinted during the remodeling of the surfaces at which the two sets of filaments are anchored. The relevance of the present analysis to the functioning of the myofibril is considered.
Actin Cytoskeleton Actins