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A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant
Author(s) -
Orlov V.N.,
Kust S.V.,
Kalmykov P.V.,
Krivosheev V.P.,
Dobrov E.N.,
Drachev V.A.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00924-7
Subject(s) - differential scanning calorimetry , tobacco mosaic virus , mutant , thermal stability , coat protein , chemistry , virus , alfalfa mosaic virus , strain (injury) , coat , rna , microbiology and biotechnology , crystallography , biophysics , biochemistry , biology , virology , gene , organic chemistry , paleontology , physics , anatomy , thermodynamics
The differential scanning calorimetry (DSC) ‘melting curves’ for virions and coat proteins (CP) of wild‐type tobacco mosaic virus (strain U1) and for its CP ts mutant ts21–66 were measured. Strain U1 and ts21–66 mutant (two amino acid substitutions in CP: I21 → T and D66 → G) differ in the type of symptoms they induce on some host plants. It was observed that CP subunits of both U1 and ts21–66 at pH 8.0, in the form of small (3–4S) aggregates, possess much lower thermal stability than in the virions. Assembly into the virus particles resulted in a DSC melting temperature increase from 41 to 72°C for U1 and from 38 to 72°C for ts21–66 CP. In the RNA‐free helical virus‐like protein assemblies U1 and ts21–66 CP subunits had a thermal stability intermediate between those in 3–4S aggregates and in the virions. ts21–66 helical protein displayed a somewhat lower thermal stability than U1.