Properties of the coat protein of a new tobacco mosaic virus coat protein ts-mutant
| Autor: | Andrey G. Solovyev, Eugeny N. Dobrov, Kust Sv, M. M. Abu-Eid, V. K. Novikov |
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| Rok vydání: | 1997 |
| Předmět: |
Circular dichroism
viruses Lysine Mutant Biology Biochemistry Capsid Tobacco Tobacco mosaic virus Cloning Molecular chemistry.chemical_classification Circular Dichroism Temperature Protein tertiary structure Amino acid Tobacco Mosaic Virus Crystallography Kinetics Plants Toxic chemistry Trinitrobenzenesulfonic Acid Mutation Ultracentrifuge Ultracentrifugation Protein Binding |
| Zdroj: | Journal of protein chemistry. 16(1) |
| ISSN: | 0277-8033 |
| Popis: | Amino acid substitutions in a majority of tobacco mosaic virus (TMV) coat protein (CP) ts-mutants have previously been mapped to the same region of the CP molecule tertiary structure, located at a distance of about 70 A from TMV virion axis. In the present work some properties of a new TMV CP ts-mutant ts21-66 (two substitutions I21 ⇒ T and D66 ⇒ G, both in the 70-A region) were studied. Thermal inactivation characteristics, sedimentation properties, circular dichroism spectra, and modification by a lysine-specific reagent, trinitrobenzensulfonic acid, of ts21–66 CP were compared with those of wild-type (U1) TMV CP. It is concluded that the 70-A region represents the most labile portion of the TMV CP molecule. Partial disordering of this region in the mutant CP at permissive temperatures leads to loss of the capacity to form two-layer aggregates of the cylindrical type, while further disordering induced by mild heating results also in the loss of the ability to form ordered helical aggregates. |
| Databáze: | OpenAIRE |
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