This study demonstrates varied morphologies in muscle proteins' coaggregation, implying implications for sarcomere function.
The morphological and structural features of coaggregates of two muscle proteins of the sarcomeric cytoskeleton (titin and myosin-binding protein C) were studied using atomic force microscopy, FTIR spectroscopy, fluorimetry using the dye thioflavin T and X-ray diffraction. It was found that, depending on the ionic strength of the solution, coaggregation of these proteins occurs with the formation of structures with different morphologies. The data obtained in vitro expand the understanding of the peculiarities of aggregation of sarcomeric muscle proteins and are important for a better understanding of their interaction in sarcomeres in vivo.
No takes yet. Share an insight, caveat, or question.
T. A. Uryupina (2025) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: