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[Study of the process of thermal aggregation of several representative tobamovirus coat proteins].

The role of the specific region of the tobacco mosaic virus (TMV) coat protein (CP) molecule (called "70A degree-region") in the regulation of ordered and unordered CP aggregation was investigated. CPs of the wild type TMV (strain U1), of temperature sensitive mutant with two amino acid substitutions in the "70A degree-region", and of cucumber virus 3 which is related to TMV but has a completely different structure in the "70A degree-region" were used. With the help of two different tests the processes of temperature-induced unordered aggregation of these three CPs were compared in solutions of different ionic strength and pH. On the basis of the data obtained it was concluded that the "70A-region" represents the most thermolabile region in the TMV CP molecule and that local thermal denaturation of this region results in unordered aggregation, when solution conditions (ionic strength and pH) favor formation of relatively large ordered aggregates (20S-"disks" or helical repolymerized protein).