The coat protein of tobacco mosaic virus forms numerous aggregates, including the small A-protein, the disk, and two helical forms. The structures of the disk, the helical protein forms, and the virus are compared. Most of the differences are in the conformation of the chain between residues 89 and
β¦ LIBER β¦
Rotational Symmetry of the Two Turn Disk Aggregate of Tobacco Mosaic Virus Protein
β Scribed by FINCH, J. T.; LEBERMAN, R.; YU-SHANG, CHANG; KLUG, A.
- Book ID
- 109653978
- Publisher
- Nature Publishing Group
- Year
- 1966
- Tongue
- English
- Weight
- 350 KB
- Volume
- 212
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/212349a0
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## Abstract The interactions of nonβionic surfactant Triton Xβ100 and the coat protein of tobacco mosaic virus, which is an established model for both ordered and nonβordered protein aggregation, were studied using turbidimetry, differential scanning calorimetry, isothermal titration calorimetry, a