title: Tailoring the Self-Assembly Behaviors of Recombinant Tobacco Mosaic Virus by Rationally Introducing Covalent Bonding at the Protein-Protein Interface.
abstract: Understanding the self-assembly mechanism of protein building blocks is important to realize the control of protein structures and functionalities. Here, for the first time, four different self-assembly behaviors of tobacco mosaic virus coat protein are reported from 2D disk arrays, disk stacks to 3D tube stacks, and tube bundles, respectively, with rationally mutated cysteines at 1, 3, and 103 sites.
authors.affiliation: Key Laboratory of Nano-Bio Interface, Division of Nanobiomedicine and i-Lab, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou, 215123, China.|University of Chinese Academy of Sciences, Beijing, 100049, China.
authors.forename: Jianting
authors.initials: J
authors.lastname: Zhang
authors.affiliation: Key Laboratory of Nano-Bio Interface, Division of Nanobiomedicine and i-Lab, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou, 215123, China.|University of Chinese Academy of Sciences, Beijing, 100049, China.
authors.forename: Kun
authors.initials: K
authors.lastname: Zhou
authors.affiliation: Key Laboratory of Nano-Bio Interface, Division of Nanobiomedicine and i-Lab, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou, 215123, China. qbwang2008@sinano.ac.cn.
authors.forename: Qiangbin
authors.initials: Q
authors.lastname: Wang
mesh_terms: D016297:Mutagenesis, Site-Directed; D010720:Phosphines / Q000494:pharmacology; D011995:Recombination, Genetic / Q000235:genetics; D014027:Tobacco Mosaic Virus / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D010720:Phosphines; D014764:Viral Proteins; C080938:tris(2-carboxyethyl)phosphine
keywords: building blocks; disulfide bonds; nanostructures; self-assembly; tobacco mosaic virus