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Motivated by the diversity and complexity of two-dimensional crystals formedby triangular proteins and protein trimers, we have investigated the structuresand phase behavior of hard-disk trimers. In order to mimic specific bindinginteractions, each trimer possesses on `attractive' disk which can interactwith similar disks on other trimers via an attractive square-well potential. Atlow density and low temperature, the fluid phase mainly consists of tetramers,pentamers, or hexamers. Hexamers provide the structural motif for ahigh-density, low-temperature periodic solid phase, but we also identify ametastable periodic structure based on a tetramer motif. At high density thereis 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.Comment: 7 pages, 6 figure

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