ArticleBiophysical journal1998
General model for lipid-mediated two-dimensional array formation of membrane proteins: application to bacteriorhodopsin.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013Review
- Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions.Biophysical journal · 2010Article
- Peripheral protein organization and its influence on lipid diffusion in biomimetic membranes.ACS chemical biology · 2010Article
- Rafts making and rafts braking: how plant flavonoids may control membrane heterogeneity.Molecular and cellular biochemistry · 2008Review
- Organization of membrane-associated proteins in lipid bilayers.The European physical journal. E, Soft matter · 2008Article
- Attraction within the membrane. Forces behind transmembrane protein folding and supramolecular complex assembly.EMBO reports · 2002Review
- A Monte Carlo study of the self-assembly of bacteriorhodopsin.Biophysical journal · 2002Article
- Segregation of photosystems in thylakoid membranes as a critical phenomenon.Biophysical journal · 2002Article
- Lipid-mediated interactions between intrinsic membrane proteins: a theoretical study based on integral equations.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on experimental evidence for 2D array formation of bacteriorhodopsin, we propose a general model for lipid-mediated 2D array formation of membrane proteins in lipid bilayers. The model includes two different lipid species, "annular" lipids and "neutral" lipids, and one protein species. The central assumption of the model is that the annular lipids interact more strongly with the protein than with the neutral lipids. Monte Carlo simulations performed on this model show that 2D arrays of proteins only form when there are annular lipids present. In addition, no arrays form if all of the lipids present are annular lipids. The geometry of the observed arrays is for the most part hexagonal. However, for a certain range of low annular lipid/protein ratios, arrays form that have geometries other than hexagonal. Using the assumption that the hydrocarbon chains of the annular lipids are restricted in motion when close to a protein, we expand the model to include a ground state and an excited state of the annular lipids. The main result from the extended model is that within a certain temperature range, increasing the temperature will lead to larger and more regular protein arrays.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.