Two-dimensional structure in a generic model of triangular proteins and protein trimers
Abstract
Motivated by the diversity and complexity of two-dimensional 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 on `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.
Cite
@article{arxiv.cond-mat/0601094,
title = {Two-dimensional structure in a generic model of triangular proteins and protein trimers},
author = {Philip J. Camp and Peter D. Duncan},
journal= {arXiv preprint arXiv:cond-mat/0601094},
year = {2009}
}
Comments
7 pages, 6 figures