Tailoring the Self‐Assembly Behaviors of Recombinant Tobacco Mosaic Virus by Rationally Introducing Covalent Bonding at the Protein–Protein Interface

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. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.