The influence of hydrogen bonding on the structure of tobacco mosaic virus (TMV) was studied by reacting dimethylsulphoxide (DMSO) with two strains of the virus (Wild-type and G-TAMV) which differ in coat-protein amino acid composition.

Reaction mixtures were spread by the Kleinschmidt technique and the samples studied in the electron microscope.

The complete particles of the two strains showed a difference in stability. Wild-type needed 74% but G-TAMV only 55% DSMO. Fragmented particles present in the original samples were uncoated by DMSO at a lower concentration than complete particles, suggesting that the ends of complete particles are particularly strongly bonded. With increasing concentrations of DMSO, G-TAMV was uncoated stepwise suggesting strong bonding between RNA and protein at certain places on the RNA.

With high enough concentrations of DMSO all particles were completely stripped leaving only RNA. The infectivity of the preparations was then the same as that of phenol-extracted RNA. The infectivity of partially stripped rods was greater than that of the completely stripped RNA but less than that of complete rods.


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