Abstract
The conformation—dependent masked state of the —SH group of the single cysteinyl residue present in the polypeptide chain of the tobacco mosaic virus (strain Vulgare) protein subunit remains preserved at the dropping mercury electrode in ammoniacal buffer (pH 9.4) containing Co(III) ions (Brdiča's solution) at 0 °C. This result has been obtained by parallel d.c. polarographic analyses and sulfhydryl tritrations in the course of the reversible denaturation of the tobacco mosaic virus protein complemented by polarographic analyses of the proteins of two tobacco mosaic virus mutants. The results obtained speek against the view that in general, the protein molecules unfold at the surface of the mercury electrode.
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