title: Early stage P22 viral capsid self-assembly mediated by scaffolding protein: atom-resolved model and molecular dynamics simulation.
abstract: Molecular dynamics simulation of an atom-resolved bacteriophage P22 capsid model is used to delineate the underlying mechanism of early stage P22 self-assembly. A dimer formed by the C-terminal fragment of scaffolding protein with a new conformation is demonstrated to catalyze capsomer (hexamer and pentamer) aggregation efficiently. Effects of scaffolding protein/coat protein binding patterns and scaffolding protein concentration on efficiency, fidelity, and capsid curvature of P22 self-assembly are identified.
authors: Center for Theoretical and Computational Nanoscience, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
authors: Jiajian
authors: J
authors: Jiang
authors: Center for Theoretical and Computational Nanoscience, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
authors: Jing
authors: J
authors: Yang
authors: Center for Theoretical and Computational Nanoscience, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
authors: Yuriy V
authors: YV
authors: Sereda
authors: Center for Theoretical and Computational Nanoscience, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
authors: Peter J
authors: PJ
authors: Ortoleva
mesh_terms: D017100:Bacteriophage P22 / Q000737:chemistry*; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D015678:Viral Structural Proteins; C111088:scaffolding protein, bacteriophage P22