TMV protein forms various discrete aggregates depending on environmental conditions such as temperature, concentration, ionic strength, and pH.
Describes the structural aggregation states of TMV protein under various biochemical conditions.
It has been known since the classical work of Schramm (1947; Schramm and Zillig, 1955) that TMV protein forms several kinds of discrete aggregates, but the relevance of these aggregates to the assembly of the complete virus from protein and RNA has not been understood. The protein is obtained in monomeric form only in fairly extreme conditions, for example at low temperature, low concentration, low ionic strength and high pH (Ansevin and Lauffer, 1959). In milder conditions the protein is usually found in the form of "A-protein" with a sedimentation coefficient about 4S, but in conditions rather more favorable for aggregation a series of larger discrete aggregates form, with sedimentation coefficients 7–8S, 18–22S, 28–33S and greater (reviewed by Caspar, 1963). The conditions favoring aggregation have been studied by Lauffer and his associates (Lauffer and Stevens, 1968) who have shown that the association of TMV protein is increased by high temperatures...
Klug et al. (Sat,) conducted a other in Tobacco Mosaic Virus (TMV) protein aggregation. TMV protein forms various discrete aggregates depending on environmental conditions such as temperature, concentration, ionic strength, and pH.