ArticleEuropean biophysics journal : EBJ2004
Size and composition of membrane protein clusters predicted by Monte Carlo analysis.
Article in European biophysics journal : EBJ, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Monte Carlo modeling of the formation and organization of ion channel clustering.PLoS computational biology · 2026Article
- Design patterns of biological cells.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- MolClustPy: a Python package to characterize multivalent biomolecular clusters.Bioinformatics (Oxford, England) · 2023Article
- Molecular Crowding and Diffusion-Capture in Synapses.iScience · 2020Article
- Excitation and adaptation in bacteria-a model signal transduction system that controls taxis and spatial pattern formation.International journal of molecular sciences · 2013Article
- Protein-coat dynamics and cluster phases in intracellular trafficking.Journal of physics. Condensed matter : an Institute of Physics journal · 2011Article
- Quantitative understanding of cell signaling: the importance of membrane organization.Current opinion in biotechnology · 2010Review
- Brownian diffusion of AMPA receptors is sufficient to explain fast onset of LTP.BMC systems biology · 2010Article
- Self-organized periodicity of protein clusters in growing bacteria.Physical review letters · 2008Article
- Computational modeling reveals molecular details of epidermal growth factor binding.BMC cell biology · 2005Article
- Clusters of interacting receptors can stabilize synaptic efficacies.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
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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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Registered trials
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