The design of proteins which associate to form ordered supramolecular assemblies is of tremendous interest for the development of novel biomaterials. Such protein biomaterials can exhibit emergent properties very different from their individual components. Theoretical studies of such assemblies on a large scale are critical for understanding and predicting the material properties of natural and designed assemblies. Here we study the large-scale dynamical properties of a designed two-dimensional protein crystal. By establishing a coarse-grained representation of the component protein, we construct a multi-resolution network model to carry out computationally tractable simulations over large time and length-scales. This system enables unique insights into the principles underlying the experimental behavior of the crystals as a whole and suggest new points of consideration for the design of new biomaterials.

Coarse-grained simulations of a coherently dynamic, two-dimensional protein crystal

251st National Meeting (2016)

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