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Tailoring the Self‐Assembly Behaviors of Recombinant Tobacco Mosaic Virus by Rationally Introducing Covalent Bonding at the Protein–Protein Interface
Author(s) -
Zhang Jianting,
Zhou Kun,
Wang Qiangbin
Publication year - 2016
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201503487
Subject(s) - tobacco mosaic virus , covalent bond , interface (matter) , recombinant dna , materials science , nanotechnology , self assembly , virus , chemistry , virology , molecule , biochemistry , biology , organic chemistry , gibbs isotherm , gene
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.