Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins

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Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. / Sperotto, M. M.; Mouritsen, O. G.

In: Biophysical Journal, Vol. 59, No. 2, 1991, p. 261-270.

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

Harvard

Sperotto, MM & Mouritsen, OG 1991, 'Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins', Biophysical Journal, vol. 59, no. 2, pp. 261-270. https://doi.org/10.1016/S0006-3495(91)82219-6

APA

Sperotto, M. M., & Mouritsen, O. G. (1991). Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. Biophysical Journal, 59(2), 261-270. https://doi.org/10.1016/S0006-3495(91)82219-6

Vancouver

Sperotto MM, Mouritsen OG. Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. Biophysical Journal. 1991;59(2):261-270. https://doi.org/10.1016/S0006-3495(91)82219-6

Author

Sperotto, M. M. ; Mouritsen, O. G. / Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. In: Biophysical Journal. 1991 ; Vol. 59, No. 2. pp. 261-270.

Bibtex

@article{c759c11f637d4ae5afae98a06659c5f0,
title = "Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins",
abstract = "Monte Carlo simulation techniques have been applied to a statistical mechanical lattice model in order to study the coherence length for the spatial fluctuations of the lipid order parameter profiles around integral membrane proteins in dipalmitoyl phosphatidylcholine bilayers. The model, which provides a detailed description of the pure lipid bilayer main transition, incorporates hydrophobic matching between the lipid and protein hydrophobic thicknesses as a major contribution to the lipid-protein interactions in lipid membranes. The model is studied at low protein-to-lipid ratios. The temperature dependence of the coherence length is found to have a dramatic peak at the phase transition temperature. The dependence on protein circumference as well as hydrophobic length is determined and it is concluded that in some cases the coherence length is much longer than previously anticipated. The long coherence length provides a mechanism for indirect lipid-mediated protein-protein long-range attraction and hence plays an important role in regulating protein segregation.",
author = "Sperotto, {M. M.} and Mouritsen, {O. G.}",
year = "1991",
doi = "10.1016/S0006-3495(91)82219-6",
language = "English",
volume = "59",
pages = "261--270",
journal = "Biophysical Society. Annual Meeting. Abstracts",
issn = "0523-6800",
publisher = "Biophysical Society",
number = "2",

}

RIS

TY - JOUR

T1 - Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins

AU - Sperotto, M. M.

AU - Mouritsen, O. G.

PY - 1991

Y1 - 1991

N2 - Monte Carlo simulation techniques have been applied to a statistical mechanical lattice model in order to study the coherence length for the spatial fluctuations of the lipid order parameter profiles around integral membrane proteins in dipalmitoyl phosphatidylcholine bilayers. The model, which provides a detailed description of the pure lipid bilayer main transition, incorporates hydrophobic matching between the lipid and protein hydrophobic thicknesses as a major contribution to the lipid-protein interactions in lipid membranes. The model is studied at low protein-to-lipid ratios. The temperature dependence of the coherence length is found to have a dramatic peak at the phase transition temperature. The dependence on protein circumference as well as hydrophobic length is determined and it is concluded that in some cases the coherence length is much longer than previously anticipated. The long coherence length provides a mechanism for indirect lipid-mediated protein-protein long-range attraction and hence plays an important role in regulating protein segregation.

AB - Monte Carlo simulation techniques have been applied to a statistical mechanical lattice model in order to study the coherence length for the spatial fluctuations of the lipid order parameter profiles around integral membrane proteins in dipalmitoyl phosphatidylcholine bilayers. The model, which provides a detailed description of the pure lipid bilayer main transition, incorporates hydrophobic matching between the lipid and protein hydrophobic thicknesses as a major contribution to the lipid-protein interactions in lipid membranes. The model is studied at low protein-to-lipid ratios. The temperature dependence of the coherence length is found to have a dramatic peak at the phase transition temperature. The dependence on protein circumference as well as hydrophobic length is determined and it is concluded that in some cases the coherence length is much longer than previously anticipated. The long coherence length provides a mechanism for indirect lipid-mediated protein-protein long-range attraction and hence plays an important role in regulating protein segregation.

U2 - 10.1016/S0006-3495(91)82219-6

DO - 10.1016/S0006-3495(91)82219-6

M3 - Journal article

C2 - 2009352

AN - SCOPUS:0026071516

VL - 59

SP - 261

EP - 270

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 2

ER -

ID: 236892888