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

P J Camp, P D Duncan

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Article number046111
Pages (from-to)-
Number of pages6
JournalPhysical Review E - Statistical, Nonlinear and Soft Matter Physics
Volume73
Issue number4
DOIs
Publication statusPublished - Apr 2006

Keywords

  • MEMBRANE-PROTEIN
  • PHASE-BEHAVIOR
  • 2 DIMENSIONS
  • MONTE-CARLO
  • ANNEXIN-V
  • TRANSPORTER
  • SIMULATION
  • SYSTEMS

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