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Modeling the phase behavior of the membrane binding protein annexin V

Modeling the phase behavior of the membrane binding protein annexin V
Modeling the phase behavior of the membrane binding protein annexin V
The bulk thermodynamic properties of proteins originate from a varied and complex combination of interactions. We propose a simple model for the formation of ordered two-dimensional aggregates based on the interactions between pairs of annexin V molecules. Simulations of this model are shown to reproduce the experimental observations of a honeycomb (p6) and a triangular (p3) crystalline phase. The simulations indicate that the transition between these two phases is first order. 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 electron microscopy and atomic force microscopy experiments.
x-ray crystallography, 2-dimensional crystallization, lipid bilayers, microscopy, crystal, aggregation, calcium
0743-7463
2988-2992
Noro, Massimo G.
87828c14-2822-494d-a664-97245d20f43c
Bates, Martin A.
6001a185-ebdb-4ed1-959c-6bba80c61ed2
Brisson, Alain
2a1869d6-fcb8-4a27-a4a5-1573cd8913d8
Frenkel, Daan
e6e79697-3c97-4493-a34c-ddc28bba3136
Noro, Massimo G.
87828c14-2822-494d-a664-97245d20f43c
Bates, Martin A.
6001a185-ebdb-4ed1-959c-6bba80c61ed2
Brisson, Alain
2a1869d6-fcb8-4a27-a4a5-1573cd8913d8
Frenkel, Daan
e6e79697-3c97-4493-a34c-ddc28bba3136

Noro, Massimo G., Bates, Martin A., Brisson, Alain and Frenkel, Daan (2002) Modeling the phase behavior of the membrane binding protein annexin V. Langmuir, 18 (8), 2988-2992. (doi:10.1021/la0156356).

Record type: Article

Abstract

The bulk thermodynamic properties of proteins originate from a varied and complex combination of interactions. We propose a simple model for the formation of ordered two-dimensional aggregates based on the interactions between pairs of annexin V molecules. Simulations of this model are shown to reproduce the experimental observations of a honeycomb (p6) and a triangular (p3) crystalline phase. The simulations indicate that the transition between these two phases is first order. 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 electron microscopy and atomic force microscopy experiments.

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More information

Published date: 16 April 2002
Keywords: x-ray crystallography, 2-dimensional crystallization, lipid bilayers, microscopy, crystal, aggregation, calcium

Identifiers

Local EPrints ID: 19831
URI: http://eprints.soton.ac.uk/id/eprint/19831
ISSN: 0743-7463
PURE UUID: 64d464a1-ec81-4be7-a9a2-12c4192e6089

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Date deposited: 22 Feb 2006
Last modified: 08 Jan 2022 01:00

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Contributors

Author: Massimo G. Noro
Author: Martin A. Bates
Author: Alain Brisson
Author: Daan Frenkel

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