[Morphological and structural studies of Sendai virus ribonucleoprotein].
The structure and morphology of Sendai virus ribonucleoprotein (RNP) with native and split protein subunits were studied by the method of circular dichroism and electron microscopy. Cleavage of the polypeptide fragment from RNP protein subunits was shown to cause changes in the secondary structure of RNP in situ but not to affect the RNP morphology; when stained with uranyl acetate both RNP types had an appearance of spiral strands.
D002942:Circular Dichroism; D008854:Microscopy, Electron; D009698:Nucleoproteins / Q000032:analysis*; D010222:Parainfluenza Virus 1, Human / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D010455:Peptides / Q000032:analysis; D011370:Proflavine / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation; D012261:Ribonucleoproteins / Q000032:analysis* / Q000378:metabolism; D014764:Viral Proteins / Q000032:analysis* / Q000378:metabolism
D009698:Nucleoproteins; D010455:Peptides; D012261:Ribonucleoproteins; D014764:Viral Proteins; D011370:Proflavine
Morfologicheskie i strukturnye issledovaniia ribonukleoproteida virusa Sendaĭ.