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dc.contributor.authorSehgal, O.P.eng
dc.contributor.authorHsu, C.H.eng
dc.contributor.corporatenameStadler Genetics Symposium (8th : 1976 : Columbia, Missouri)eng
dc.date.issued1976eng
dc.description.abstractVirions of southern bean mosaic virus (SBMV), a small RNA-containing isometric plant virus, are stabilized with strong linkages between the coat protein subunits mediated through divalent metal ions (magnesium, calcium) and hydrophobic interactions. Virion treatments interfering with these inter-subunit linkages markedly alter the conformation and stability of the SBMV capsid. The virion capsid is composed of the entire complement of the viral protein, including a small proportion of stable coat protein dimers formed with covalent linkages between the epsilon-amino groups of the lysyl residues. The viral RNA is located within the capsid but 'loosely' contacts only one-third of the total coat protein. A tentative structural model of SBMV virions based upon physico-chemical and morphological considerations is proposed.eng
dc.description.statementofresponsibilityO. P. SEHGAL and C.H. HSU, Department of Plant Pathology, University of Missouri, Columbia, MO.eng
dc.identifier.urihttps://hdl.handle.net/10355/66586
dc.languageEnglisheng
dc.publisherUniversity of Missouri, Agricultural Experiment Stationeng
dc.titleRNA : protein and protein : Protein interactions in the virions of southern bean mosaic virus : (isometric plant viruses, stabilizing interactions, capsid structure)eng
dc.typeChaptereng


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