Two-dimensional structure in a generic model of triangular proteins and protein trimers.

Motivated by the diversity and complexity of two-dimensional (2D) crystals formed by triangular proteins and protein trimers, we have investigated the structures and phase behavior of hard-disk trimers. In order to mimic specific binding interactions, each trimer possesses an "attractive" disk which can interact with similar disks on other trimers via an attractive square-well potential. At low density and low temperature, the fluid phase mainly consists of tetramers, pentamers, or hexamers. Hexamers provide the structural motif for a high-density, low-temperature periodic solid phase, but we also identify a metastable periodic structure based on a tetramer motif. At high density there is a transition between orientationally ordered and disordered solid phases. The connections between simulated structures and those of 2D protein crystals--as seen in electron microscopy--are briefly discussed.