β Scribed by Stubbs, Gerald ;Warren, Stephen ;Mandelkow, Eckhard
No coin nor oath required. For personal study only.
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 1 13, which lies in the region of protein at the center of the virus, inside the RNA. It is disordered in the disk, but has a fixed conformation in the virus and the protein helices. The differences between the virus and the two helical protein forms are largely in the conformations of arginines and carboxylic acids in this region.
π SIMILAR VOLUMES
## 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