Polymerization studies on protein from the dahlemense strain of tobacco mosaic virus: Light scattering and related studies

Abstract Light-scattering and related studies on the polymerization behavior of the protein from the PM2 strain of TMV show that in phosphate buffer of ionic strength 0.1, the maximum extent of temperature-mediated polymerization occurs at pH values lower than in the case of TMV protein. The pH range of temperature-induced polymerization is from 5.0 to 6.0, contrasted with 5.0 to 7.5 for TMV protein. Velocity sedimentation studies show that PM2 protein at room temperature in phosphate buffer ( I = 0.1) has sedimentation coefficients of 174 S, 104 S, and 4.3 S at pH values of 4.89, 5.53, and 7.5. Electron microscope studies show that at room temperature in phosphate buffer of 0.1 ionic strength at pH 5.53, PM2 protein has structures resembling essentially that of stacked double discs with an occasional helical structure. Similar studies of PM2 protein in 0.1 M ammonium acetate buffer at pH 5.2 show single, double, and double-double helices.