Abstract
The results of the study of the structure of two related rod-like viruses, tobacco mosaic virus and cucumber virus 4, by laser Raman spectroscopy are presented. It is found that the structure of the protein subunits of the two viruses differ significantly: the TMV protein has more α-helix and less β-structure than the CV protein. All tryptophan residues in the proteins of both viruses are buried in the hydrophobic environment, and out of the four tyrosine residues present in both proteins, two participate in strong H-binding with COO −-groups of acidic amino acids and the two others are exposed to the solvent. Intravirus RNAs of both viruses have the same structure of sugar-phosphate backbone, characterised by the simultaneous presence of at least two different conformations of phosphodiester bonds and of ribose residues. The degree of base stacking in the two intravirus RNAs is much smaller than in helical regions of free RNAs.
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