Abstract
Biological membranes contain a high density of protein molecules, many of which associate into two-dimensional microdomains with important physiological functions. We have used Monte Carlo simulations to examine the self-association of idealized protein species in two dimensions. The proteins have defined bond strengths and bond angles, allowing us to estimate the size and composition of the aggregates they produce at equilibrium. With a single species of protein, the extent of cluster formation and the sizes of individual clusters both increase in non-linear fashion, showing a “phase change” with protein concentration and bond strength. With multiple co-aggregating proteins, we find that the extent of cluster formation also depends on the relative proportions of participating species. For some lattice geometries, a stoichiometric excess of particular species depresses cluster formation and moreover distorts the composition of clusters that do form. Our results suggest that the self-assembly of microdomains might require a critical level of subunits and that for optimal co-aggregation, proteins should be present in the membrane in the correct stoichiometric ratios.
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Acknowledgements
We are grateful to Matthew Levin for useful suggestions. Supported by NIGMS grant GM64713.
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Goldman, J., Andrews, S. & Bray, D. Size and composition of membrane protein clusters predicted by Monte Carlo analysis. Eur Biophys J 33, 506–512 (2004). https://doi.org/10.1007/s00249-004-0391-6
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DOI: https://doi.org/10.1007/s00249-004-0391-6