[Circular dichroism study of the ribonucleoprotein structure of Sendai virus isolated from infected chick embryo cells].

Thermostability and secondary structure of RNA, a component of ribonucleoprotein (RNP) of Sendai virus isolated from infected chick embryo cells (cRNP) and from virions (vRNP) were studied by the method of circular dichroism. The secondary structure of RNA in cRNP was shown to be practically no different from that of free RNA whereas incorporation of RNA into vRNP was accompanied by a significant decrease in the number of paired bases in it. Comparison of thermodenaturation parameters of cRNP and vRNP also revealed significant differences in their structural organization. Thus, melting of cRNP as well as of free RNA is of markedly non-cooperative nature indicating poor RNA-protein interactions in the complex. In contrast, the process of vRNP thermodenaturation occurs in a step-wise manner in a narrow temperature range indicating a significant role in the maintenance of this RNP structure of both RNA-protein and, apparently, protein-protein interactions.