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Computer simulation of the phase behavior of a model membrane protein: Annexin V

Computer simulation of the phase behavior of a model membrane protein: Annexin V
Computer simulation of the phase behavior of a model membrane protein: Annexin V
The bulk thermodynamic properties of membrane proteins originate from a complex combination of molecular interactions. We propose a simple model based on the pair interactions between a model membrane protein, annexin V. The experimental observations of a honeycomb (p6) and a triangular (p3) phase are successfully reproduced with Monte Carlo computer simulations. Grand canonical simulations and a newly developed "strip"-move constant pressure technique reveal the stability of a dilute fluid phase and a dense solid phase, not observed with the current experimental technology. While this model is extremely simple in that it relies only on hard-body and short-range directional interactions, it nevertheless captures the essential physics of the interactions between the protein molecules and reproduces the phase behavior observed in experiments.
2-dimensional crystallization, microscopy
0021-9606
7217-7224
Bates, Martin A.
6001a185-ebdb-4ed1-959c-6bba80c61ed2
Noro, Massimo G.
87828c14-2822-494d-a664-97245d20f43c
Frenkel, Daan
e6e79697-3c97-4493-a34c-ddc28bba3136
Bates, Martin A.
6001a185-ebdb-4ed1-959c-6bba80c61ed2
Noro, Massimo G.
87828c14-2822-494d-a664-97245d20f43c
Frenkel, Daan
e6e79697-3c97-4493-a34c-ddc28bba3136

Bates, Martin A., Noro, Massimo G. and Frenkel, Daan (2002) Computer simulation of the phase behavior of a model membrane protein: Annexin V. The Journal of Chemical Physics, 116 (16), 7217-7224. (doi:10.1063/1.1463423).

Record type: Article

Abstract

The bulk thermodynamic properties of membrane proteins originate from a complex combination of molecular interactions. We propose a simple model based on the pair interactions between a model membrane protein, annexin V. The experimental observations of a honeycomb (p6) and a triangular (p3) phase are successfully reproduced with Monte Carlo computer simulations. Grand canonical simulations and a newly developed "strip"-move constant pressure technique reveal the stability of a dilute fluid phase and a dense solid phase, not observed with the current experimental technology. While this model is extremely simple in that it relies only on hard-body and short-range directional interactions, it nevertheless captures the essential physics of the interactions between the protein molecules and reproduces the phase behavior observed in experiments.

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More information

Published date: 22 April 2002
Keywords: 2-dimensional crystallization, microscopy
Organisations: Chemistry

Identifiers

Local EPrints ID: 19669
URI: http://eprints.soton.ac.uk/id/eprint/19669
ISSN: 0021-9606
PURE UUID: afb8c2d9-7fa8-41bf-b3d6-b85bf35fa8e7

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Date deposited: 16 Feb 2006
Last modified: 15 Jul 2019 19:26

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