Abstract
The protein of TMV polymerizes slowly in alkaline solution (pH 8–10.5) to form rod-shaped particles which have the stacked-disk structure. The polymerization process has been followed by electron microscopy and analytical centrifugation; possible mechanisms are discussed. The particles are resistant to changes in buffer concentration and pH, and are not in equilibrium with their precursors. They are degraded only at a pH above 12 or below 2 and are resistant to proteolytic enzymes. Electrophoresis indicates that the particles consist of more than one structural type.
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