Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers

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Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers. / Sperotto, Maria M.; Mouritsen, Ole G.

In: European Biophysics Journal, Vol. 22, No. 5, 1993, p. 323-328.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sperotto, MM & Mouritsen, OG 1993, 'Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers', European Biophysics Journal, vol. 22, no. 5, pp. 323-328. https://doi.org/10.1007/BF00213555

APA

Sperotto, M. M., & Mouritsen, O. G. (1993). Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers. European Biophysics Journal, 22(5), 323-328. https://doi.org/10.1007/BF00213555

Vancouver

Sperotto MM, Mouritsen OG. Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers. European Biophysics Journal. 1993;22(5):323-328. https://doi.org/10.1007/BF00213555

Author

Sperotto, Maria M. ; Mouritsen, Ole G. / Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers. In: European Biophysics Journal. 1993 ; Vol. 22, No. 5. pp. 323-328.

Bibtex

@article{4767c6d1c7334ac7991dd8cd2834163b,
title = "Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers",
abstract = "A model recently used to study lipid-protein interactions in one-component lipid bilayers (Sperotto and Mouritsen, 1991 a, b) has been extended in order to include two different lipid species characterized by different acyl-chain lengths. The model, which is a statistical mechanical lattice model, assumes that hydrophobic matching between lipid-bilayer hydrophobic thickness and hydrophobic length of the integral protein is an important aspect of the interactions. By means of Monte Carlo simulation techniques, the lateral distribution of the two lipid species near the hydrophobic protein-lipid interface in the fluid phase of the bilayer has been derived. The results indicate that there is a very structured and heterogeneous distribution of the two lipid species near the protein and that the protein-lipid interface is enriched in one of the lipid species. Out of equilibrium, the concentration profiles of the two lipid species away from the protein interface are found to develop a long-range oscillatory behavior. Such dynamic membrane heterogeneity may be of relevance for determining the physical factors involved in lipid specificity of protein function.",
keywords = "Binary mixture, Lipid bilayer, Lipid selectivity, Lipidprotein interaction",
author = "Sperotto, {Maria M.} and Mouritsen, {Ole G.}",
year = "1993",
doi = "10.1007/BF00213555",
language = "English",
volume = "22",
pages = "323--328",
journal = "European Biophysics Journal",
issn = "0175-7571",
publisher = "Springer",
number = "5",

}

RIS

TY - JOUR

T1 - Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers

AU - Sperotto, Maria M.

AU - Mouritsen, Ole G.

PY - 1993

Y1 - 1993

N2 - A model recently used to study lipid-protein interactions in one-component lipid bilayers (Sperotto and Mouritsen, 1991 a, b) has been extended in order to include two different lipid species characterized by different acyl-chain lengths. The model, which is a statistical mechanical lattice model, assumes that hydrophobic matching between lipid-bilayer hydrophobic thickness and hydrophobic length of the integral protein is an important aspect of the interactions. By means of Monte Carlo simulation techniques, the lateral distribution of the two lipid species near the hydrophobic protein-lipid interface in the fluid phase of the bilayer has been derived. The results indicate that there is a very structured and heterogeneous distribution of the two lipid species near the protein and that the protein-lipid interface is enriched in one of the lipid species. Out of equilibrium, the concentration profiles of the two lipid species away from the protein interface are found to develop a long-range oscillatory behavior. Such dynamic membrane heterogeneity may be of relevance for determining the physical factors involved in lipid specificity of protein function.

AB - A model recently used to study lipid-protein interactions in one-component lipid bilayers (Sperotto and Mouritsen, 1991 a, b) has been extended in order to include two different lipid species characterized by different acyl-chain lengths. The model, which is a statistical mechanical lattice model, assumes that hydrophobic matching between lipid-bilayer hydrophobic thickness and hydrophobic length of the integral protein is an important aspect of the interactions. By means of Monte Carlo simulation techniques, the lateral distribution of the two lipid species near the hydrophobic protein-lipid interface in the fluid phase of the bilayer has been derived. The results indicate that there is a very structured and heterogeneous distribution of the two lipid species near the protein and that the protein-lipid interface is enriched in one of the lipid species. Out of equilibrium, the concentration profiles of the two lipid species away from the protein interface are found to develop a long-range oscillatory behavior. Such dynamic membrane heterogeneity may be of relevance for determining the physical factors involved in lipid specificity of protein function.

KW - Binary mixture

KW - Lipid bilayer

KW - Lipid selectivity

KW - Lipidprotein interaction

U2 - 10.1007/BF00213555

DO - 10.1007/BF00213555

M3 - Journal article

C2 - 8112219

AN - SCOPUS:0027438092

VL - 22

SP - 323

EP - 328

JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

IS - 5

ER -

ID: 236891135