The organization of potato virus X coat proteins in virus particles studied by tritium planigraphy and model building

• Published in: Virology (New York, N.Y.) Vol. 188; no. 1; pp. 175 - 180
• Main Authors: Baratova, L.A., Grebenshchikov, N.I., Dobrov, E.N., Gedrovich, A.V., Kashirin, I.A., Shishkov, A.V., Efimov, A.V., Järvekülg, L., Radavsky, Yu.L., Saarma, M.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 01.05.1992; Elsevier
• Subjects: Amino Acid Sequence; Biological and medical sciences; Capsid - chemistry; Fundamental and applied biological sciences. Psychology; Microbiology; Models, Molecular; Molecular Sequence Data; Morphology, structure, chemical composition, physicochemical properties; Nicotiana; Plant Viruses - chemistry; Plants, Toxic; potato virus X; POTEXVIRUS; Protein Conformation; PROTEINAS; PROTEINE; TECHNIQUE ANALYTIQUE; TECNICAS ANALITICAS; Tomography, X-Ray; Tritium; Virology; VIRUS DE LAS PLANTAS; VIRUS DES VEGETAUX; Plant pathogen; Tertiary structure; Potexvirus; Tritium; Subunit; Virus; Proteins; Virion; Potato virus X; Proton irradiation; Models; Capsid; Virus surface

Potato virus X particles containing the intact, undegraded Ps form of the coat protein and particles containing the in situ degraded Pf form of the coat protein, which is devoid of 19–21 amino acids from the N-terminus, were bombarded with thermally activated tritium atoms, and the intramolecular di...