Jiang Jiajian, Yang Jing, Sereda Yuriy V, Ortoleva Peter J
Center for Theoretical and Computational Nanoscience, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
J Phys Chem B. 2015 Apr 23;119(16):5156-62. doi: 10.1021/acs.jpcb.5b00303. Epub 2015 Apr 9.
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.
利用原子分辨噬菌体P22衣壳模型的分子动力学模拟来阐明P22早期自组装的潜在机制。由具有新构象的支架蛋白C末端片段形成的二聚体被证明能有效催化衣壳粒（六聚体和五聚体）聚集。确定了支架蛋白/衣壳蛋白结合模式和支架蛋白浓度对P22自组装效率、保真度和衣壳曲率的影响。
