Steady-state compartmentalization of lipid membranes by active proteins

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Steady-state compartmentalization of lipid membranes by active proteins. / Sabra, Mads C.; Mouritsen, Ole G.

In: Biophysical Journal, Vol. 74, No. 2 I, 02.1998, p. 745-752.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Sabra, MC & Mouritsen, OG 1998, 'Steady-state compartmentalization of lipid membranes by active proteins', Biophysical Journal, vol. 74, no. 2 I, pp. 745-752. https://doi.org/10.1016/S0006-3495(98)73999-2

APA

Sabra, M. C., & Mouritsen, O. G. (1998). Steady-state compartmentalization of lipid membranes by active proteins. Biophysical Journal, 74(2 I), 745-752. https://doi.org/10.1016/S0006-3495(98)73999-2

Vancouver

Sabra MC, Mouritsen OG. Steady-state compartmentalization of lipid membranes by active proteins. Biophysical Journal. 1998 Feb;74(2 I):745-752. https://doi.org/10.1016/S0006-3495(98)73999-2

Author

Sabra, Mads C. ; Mouritsen, Ole G. / Steady-state compartmentalization of lipid membranes by active proteins. In: Biophysical Journal. 1998 ; Vol. 74, No. 2 I. pp. 745-752.

Bibtex

@article{6866b241b6104d14a34f73b8a031e23e,
title = "Steady-state compartmentalization of lipid membranes by active proteins",
abstract = "Using a simple microscopic model of lipid-protein interactions, based on the hydrophobic matching principle we study some generic aspects of lipid- membrane compartmentalization controlled by a dispersion of active integral membrane proteins. The activity of the proteins is simulated by conformational excitations governed by an external drive, and the deexcitation is controlled by interaction of the protein with its lipid surroundings. In response to the flux of energy into the proteins from the environment and the subsequent dissipation of energy into the lipid bilayer, the lipid-protein assembly reorganizes into a steady-state structure with a typical length scale determined by the strength of the external drive. In the specific case of a mixed dimyristoylphosphatidylcholine- distearoylphosphatidylcholine bilayer in the gel-fluid coexistence region, it is shown explicitly by computer simulation that the activity of an integral membrane protein can lead to a compartmentalization of the lipid-bilayer membrane. The compartmentalization is related to the dynamical process of phase separation and lipid domain formation.",
author = "Sabra, {Mads C.} and Mouritsen, {Ole G.}",
year = "1998",
month = "2",
doi = "10.1016/S0006-3495(98)73999-2",
language = "English",
volume = "74",
pages = "745--752",
journal = "Biophysical Society. Annual Meeting. Abstracts",
issn = "0523-6800",
publisher = "Biophysical Society",
number = "2 I",

}

RIS

TY - JOUR

T1 - Steady-state compartmentalization of lipid membranes by active proteins

AU - Sabra, Mads C.

AU - Mouritsen, Ole G.

PY - 1998/2

Y1 - 1998/2

N2 - Using a simple microscopic model of lipid-protein interactions, based on the hydrophobic matching principle we study some generic aspects of lipid- membrane compartmentalization controlled by a dispersion of active integral membrane proteins. The activity of the proteins is simulated by conformational excitations governed by an external drive, and the deexcitation is controlled by interaction of the protein with its lipid surroundings. In response to the flux of energy into the proteins from the environment and the subsequent dissipation of energy into the lipid bilayer, the lipid-protein assembly reorganizes into a steady-state structure with a typical length scale determined by the strength of the external drive. In the specific case of a mixed dimyristoylphosphatidylcholine- distearoylphosphatidylcholine bilayer in the gel-fluid coexistence region, it is shown explicitly by computer simulation that the activity of an integral membrane protein can lead to a compartmentalization of the lipid-bilayer membrane. The compartmentalization is related to the dynamical process of phase separation and lipid domain formation.

AB - Using a simple microscopic model of lipid-protein interactions, based on the hydrophobic matching principle we study some generic aspects of lipid- membrane compartmentalization controlled by a dispersion of active integral membrane proteins. The activity of the proteins is simulated by conformational excitations governed by an external drive, and the deexcitation is controlled by interaction of the protein with its lipid surroundings. In response to the flux of energy into the proteins from the environment and the subsequent dissipation of energy into the lipid bilayer, the lipid-protein assembly reorganizes into a steady-state structure with a typical length scale determined by the strength of the external drive. In the specific case of a mixed dimyristoylphosphatidylcholine- distearoylphosphatidylcholine bilayer in the gel-fluid coexistence region, it is shown explicitly by computer simulation that the activity of an integral membrane protein can lead to a compartmentalization of the lipid-bilayer membrane. The compartmentalization is related to the dynamical process of phase separation and lipid domain formation.

UR - http://www.scopus.com/inward/record.url?scp=0031903860&partnerID=8YFLogxK

U2 - 10.1016/S0006-3495(98)73999-2

DO - 10.1016/S0006-3495(98)73999-2

M3 - Journal article

C2 - 9533687

AN - SCOPUS:0031903860

VL - 74

SP - 745

EP - 752

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 2 I

ER -

ID: 236886397