STRUCTURE OF CONNECTOR COMPLEX OF SPP I
$9,722P41FY2000RRNIH
Brookhaven Science Assoc-Brookhaven Lab, Upton NY
Investigators
Linked publications & trials
Paper 25242887Paper 24793749Paper 20887859Paper 20155329Paper 18814851Paper 18639797Paper 18154334Paper 18006331Paper 17688395Paper 17548765Paper 16203986Paper 15567868Paper 15208690Paper 14557074Paper 12972252Paper 12498796Paper 12379108Paper 12367530Paper 12064938Paper 12008948Paper 11851882Paper 11703654Paper 11562162Paper 11357616Paper 11290566Paper 11278978Paper 11222712Paper 11222698Paper 11170476Paper 11148208Paper 10908577Paper 10677495
Abstract
The portal protein of bacteriophage SPPl,.gp6, is a large homo-oligomer of 13 subunits. The connector (head/tail) is composed of the portal protein plus three other proteins. Masses are being determined for the portal protein alone, for a gp6tgp7 complex (the gp7 seems to bind in the hole af the portal), and for the whole connector complex, in order to determine the stoichiometry of the more minor proteins. The samples looked good, but the m analysis is not finished.
View original record on NIH RePORTER →