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.

Keywords: building blocks; disulfide bonds; nanostructures; self-assembly; tobacco mosaic virus.