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TMV vulgare, A 14, Ni 725; Two-and Three-Layer Aggregates, Structural and Mechanistic Differences, Inter-Subunit Interactions, Non-Specific Aggregations The aggregation behaviour of tobacco mosaic virus (TMV) protein vulgare was compared to that of two mutants, A 14 and Ni725, with amino acid exchanges localized in the coat protein at posi­ tions 107 (Thr → Met, in N i725) and 129 (lie → Thr, in both mutants). This behaviour, as meas­ ured by sedimentation, hydrogen ion titration, light-scattering, and near-UV absorption difference and circular dichroism (CD) spectroscopy, differs characteristically both in the range of the A-protein (pH 8) and near neutrality, whereas nuclear magnetic resonance (NMR) and far-UV CD point at only subtle, or no structural differences between the three strains.

The Mechanism of Aggregation of the Coat Protein of Tobacco Mosaic Virus. A Comparative Study on Vulgare and Mutant Proteins