[Investigation of helical plant virus ribonucleoprotein structures with the help of tritium planigraphy and theoretical modeling].
The results of the studies of helical plant virus structures by tritium planigraphy (TP) method are discussed. TP method is based on bombardment of macromolecular objects with a stream of tritium atoms, followed by analysis of tritium label distribution along the macromolecule. By combining the TP data with the results of theoretical predictions of the protein structure, it turned out to be possible to propose a model of the coat protein structure in the virions of potato virus X (the type member of potexvirus group) and potato virus A (one of the members of potyvirus group). With the help of TP it also managed to find subtle differences in the coat protein structure between wildtype tobacco mosaic virus (strain U1) and its mutant with two amino acid substitutions in the coat protein and alter host specificity.
Dobrov
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EN
Efimov
A V
AV
Baratova
L A
LA
D036022:Capsid Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009029:Mosaic Viruses / Q000737:chemistry; D010942:Plant Viruses / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012261:Ribonucleoproteins / Q000737:chemistry*; D014316:Tritium
D036022:Capsid Proteins; D012261:Ribonucleoproteins; D014316:Tritium