Visualizing the emergence of order during self-assembly of protein nanorods

Protein scaffolds, such as collagen fibrils, provide the template for generating macromolecular-inorganic hybrid structures. The production of synthetic protein templates would allow scientists to create materials with precise control over spatial arrangement and morphology. However, how to program intermolecular interactions to tune the order of synthetic protein templates is still not crystal.
In this presentation, I will share recent results in the effort to build 2D protein liquid crystal with long-range order from computationally designed protein nanorods. I further utilize in-situ video-rate, single-molecule atomic force microscopy to observe the assembly of these proteins into two-dimensional matrices. With this technique, I can directly observe dynamics of single-molecules, moving, reorienting, and generating extended crystalline order. With the help of molecular dynamic simulation, I am able to investigate how protein-protein interactions, protein-substrate interactions influence the overall assembly dynamics. Indeed, in many cases, it is entropy, both solute entropy and osmotic pressure, rather than enthalpy, formation of chemical bonds, to determine the phases of protein self-assembly matrix, from highly dense liquid to isotropic to liquid crystal to crystal.