Abstract
The first attempt has been made to suggest a model of influenza A virus matrix M1 protein spatial structure and molecule orientation within a virion on the basis of tritium planigraphy data and theoretical prediction results. Limited in situ proteolysis of the intact virions with bromelain and surface plasmon resonance spectroscopy study of the M1 protein interaction with lipid coated surfaces were used for independent confirmation of the proposed model.
Keywords: Influenza A virus, matrix M1 protein, secondary structure prediction, tritium planigraphy, surface plasmon resonance spectroscopy, three-dimensional modeling