title: A T = 1 capsid formed by protein of brome mosaic virus in the presence of trypsin.
abstract: In the presence of trypsin, the coat protein of brome mosaic virus (BMV) has been observed to polymerize in a D2O buffer at pD 7.6 to form a small empty capsid with triangulation number T = 1. Normally, this same protein polymerizes at acidic pH to form empty capsids with T = 3. The trypsin is shown to remove 63 amino acids on the N terminus side leaving a polypeptide chain of Mr 13,500. The kinetics of formation of this small particle have been followed by neutron scattering. Further, the particle has been characterized by various physical methods: analytical centrifugation, quasielastic light scattering, and neutron scattering. It is found to have a radius of about 85-90 A, and a molecular weight of 760,000, in fair agreement with the value expected for a particle made of 60 subunits of 13,500.
authors.affiliation: Institut Laue-Langevin, 156X Centre de Tri, 38042 Grenoble Cédex, France.
authors.forename: M
authors.initials: M
authors.lastname: Cuillel
authors.forename: B
authors.initials: B
authors.lastname: Jacrot
authors.forename: M
authors.initials: M
authors.lastname: Zulauf