C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES ON TOBACCO MOSAIC-VIRUS AND ITS PROTEIN

Fourier transform nuclear magnetic resonance studies on 12% 13C-enriched tobacco mosaic virus (TMV) and its rod-like protein oligomers in solution with molecular weights up to 42 × 106 are reported. In the virus ~ 17% of the cartons of the protein subunit have line widths of 5300 Hz and T1, ≤ 1 s and are concluded to be mobile with more than one degree of freedom of internal rotation about a carbon-carbon bond. In the rodlike polymer of TMV protein at pH 5.3, 30% of the carbons are mobile, which implies rotational motions about carbon-carbon bonds and/or motions of the protein subunits within the polymer. The presence of internal mobility is supported by the observation that 20% of the carbons in the double disklike oligomer show decreasing line width upon increasing temperature; the remaining resonances have line widths which are temperature independent during the double disklike polymerization process. Since the molecular weight of TMV protein polymers increases with increasing temperature, this demonstrates that all nuclei within the double disklike oligomer are mobile. NMR and X-ray data on the double disklike polymer reveal differences with respect to internal mobility. © 1979, American Chemical Society. All rights reserved.