Title of article :
Domain Study of Bacteriophage P22 Coat Protein and Characterization of the Capsid Lattice Transformation by Hydrogen/Deuterium Exchange Original Research Article
Author/Authors :
Sebyung Kang، نويسنده , , Peter E. Prevelige Jr، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Abstract :
Viral capsids are dynamic structures which undergo a series of structural transformations to form infectious viruses. The dsDNA bacteriophage P22 is used as a model system to study the assembly and maturation of icosahedral dsDNA viruses. The P22 procapsid, which is the viral capsid precursor, is assembled from coat protein with the aid of scaffolding protein. Upon DNA packaging, the capsid lattice expands and becomes a stable virion. Limited proteolysis and biochemical experiments indicated that the coat protein consists of two domains connected by a flexible loop.
Keywords :
bacteriophage P22 , hydrogen/deuterium exchange , capsid maturation , mass spectrometry
Journal title :
Journal of Molecular Biology
Journal title :
Journal of Molecular Biology