Mattress model of lipid-protein interactions in membranes

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

Standard

Mattress model of lipid-protein interactions in membranes. / Mouritsen, Ole G.; Bloom, Myer.

In: Biophysical Journal, Vol. 46, No. 2, 1984, p. 141-153.

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

Harvard

Mouritsen, OG & Bloom, M 1984, 'Mattress model of lipid-protein interactions in membranes', Biophysical Journal, vol. 46, no. 2, pp. 141-153. https://doi.org/10.1016/S0006-3495(84)84007-2

APA

Mouritsen, O. G., & Bloom, M. (1984). Mattress model of lipid-protein interactions in membranes. Biophysical Journal, 46(2), 141-153. https://doi.org/10.1016/S0006-3495(84)84007-2

Vancouver

Mouritsen OG, Bloom M. Mattress model of lipid-protein interactions in membranes. Biophysical Journal. 1984;46(2):141-153. https://doi.org/10.1016/S0006-3495(84)84007-2

Author

Mouritsen, Ole G. ; Bloom, Myer. / Mattress model of lipid-protein interactions in membranes. In: Biophysical Journal. 1984 ; Vol. 46, No. 2. pp. 141-153.

Bibtex

@article{26328db238524fdd8ff76d37d9e06a3c,
title = "Mattress model of lipid-protein interactions in membranes",
abstract = "A thermodynamic model is proposed for describing phase diagrams of mixtures of lipid bilayers and amphiphilic proteins or polypeptides in water solution. The basic geometrical variables of the model are the thickness of the hydrophobic region of the lipid bilayer and the length of the hydrophobic region of the proteins. The model incorporates the elastic properties of the lipid bilayer and the proteins, as well as indirect and direct lipid-protein interactions expressed in terms of the geometrical variables. The concept of mismatch of the hydrophobic regions of the lipids and proteins is an important ingredient of the model. The general phase behavior is calculated using simple real solution theory. The phase behavior turns out to be quite rich and is used to discuss previous experiments on planar aggregations of proteins in phospholipid bilayers and to propose a systematic study of synthetic amphiphilic polypeptides in bilayers of different thicknesses. The model is used to interpret the influence of the lipid-protein interaction on calorimetric measurements and on local orientational order as determined by deuterium nuclear magnetic resonance.",
author = "Mouritsen, {Ole G.} and Myer Bloom",
year = "1984",
doi = "10.1016/S0006-3495(84)84007-2",
language = "English",
volume = "46",
pages = "141--153",
journal = "Biophysical Society. Annual Meeting. Abstracts",
issn = "0523-6800",
publisher = "Biophysical Society",
number = "2",

}

RIS

TY - JOUR

T1 - Mattress model of lipid-protein interactions in membranes

AU - Mouritsen, Ole G.

AU - Bloom, Myer

PY - 1984

Y1 - 1984

N2 - A thermodynamic model is proposed for describing phase diagrams of mixtures of lipid bilayers and amphiphilic proteins or polypeptides in water solution. The basic geometrical variables of the model are the thickness of the hydrophobic region of the lipid bilayer and the length of the hydrophobic region of the proteins. The model incorporates the elastic properties of the lipid bilayer and the proteins, as well as indirect and direct lipid-protein interactions expressed in terms of the geometrical variables. The concept of mismatch of the hydrophobic regions of the lipids and proteins is an important ingredient of the model. The general phase behavior is calculated using simple real solution theory. The phase behavior turns out to be quite rich and is used to discuss previous experiments on planar aggregations of proteins in phospholipid bilayers and to propose a systematic study of synthetic amphiphilic polypeptides in bilayers of different thicknesses. The model is used to interpret the influence of the lipid-protein interaction on calorimetric measurements and on local orientational order as determined by deuterium nuclear magnetic resonance.

AB - A thermodynamic model is proposed for describing phase diagrams of mixtures of lipid bilayers and amphiphilic proteins or polypeptides in water solution. The basic geometrical variables of the model are the thickness of the hydrophobic region of the lipid bilayer and the length of the hydrophobic region of the proteins. The model incorporates the elastic properties of the lipid bilayer and the proteins, as well as indirect and direct lipid-protein interactions expressed in terms of the geometrical variables. The concept of mismatch of the hydrophobic regions of the lipids and proteins is an important ingredient of the model. The general phase behavior is calculated using simple real solution theory. The phase behavior turns out to be quite rich and is used to discuss previous experiments on planar aggregations of proteins in phospholipid bilayers and to propose a systematic study of synthetic amphiphilic polypeptides in bilayers of different thicknesses. The model is used to interpret the influence of the lipid-protein interaction on calorimetric measurements and on local orientational order as determined by deuterium nuclear magnetic resonance.

U2 - 10.1016/S0006-3495(84)84007-2

DO - 10.1016/S0006-3495(84)84007-2

M3 - Journal article

C2 - 6478029

AN - SCOPUS:0021474573

VL - 46

SP - 141

EP - 153

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 2

ER -

ID: 238388339