Tritium planigraphy and nanosized biological particles

Advances in studies of protein and complex biological systems by tritium planigraphy are considered. Particular attention is paid to detailing the structural organization of the protein components of the influenza virus. The structure of the M1 protein in a solution, virion, and crystal is analyzed. The specific features of this protein identified using tritium planigraphy and computer simulation are indicative of significant changes in its conformation depending on the “phase” state. Models of the spatial structure of the M1 protein in solution and in the virion are proposed. Structural disorder is observed in one of the three domains of this protein. Ideas on the importance of this structure for the multifunctional properties of the protein, such as binding to the membrane and a ribonucleoprotein complex, as well as the transfer of genetic material during viral infection of healthy cells, were suggested.