Wetting and capillary condensation as means of protein organization in membranes

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Wetting and capillary condensation as means of protein organization in membranes. / Gil, Tamir; Sabra, Mads C.; Ipsen, John Hjort; Mouritsen, Ole G.

In: Biophysical Journal, Vol. 73, No. 4, 10.1997, p. 1728-1741.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Gil, T, Sabra, MC, Ipsen, JH & Mouritsen, OG 1997, 'Wetting and capillary condensation as means of protein organization in membranes', Biophysical Journal, vol. 73, no. 4, pp. 1728-1741. https://doi.org/10.1016/S0006-3495(97)78204-3

APA

Gil, T., Sabra, M. C., Ipsen, J. H., & Mouritsen, O. G. (1997). Wetting and capillary condensation as means of protein organization in membranes. Biophysical Journal, 73(4), 1728-1741. https://doi.org/10.1016/S0006-3495(97)78204-3

Vancouver

Gil T, Sabra MC, Ipsen JH, Mouritsen OG. Wetting and capillary condensation as means of protein organization in membranes. Biophysical Journal. 1997 Oct;73(4):1728-1741. https://doi.org/10.1016/S0006-3495(97)78204-3

Author

Gil, Tamir ; Sabra, Mads C. ; Ipsen, John Hjort ; Mouritsen, Ole G. / Wetting and capillary condensation as means of protein organization in membranes. In: Biophysical Journal. 1997 ; Vol. 73, No. 4. pp. 1728-1741.

Bibtex

@article{31e85cb71c524723814e7e47b2ffcf1d,
title = "Wetting and capillary condensation as means of protein organization in membranes",
abstract = "Wetting and capillary condensation are thermodynamic phenomena in which the special affinity of interfaces to a thermodynamic phase, relative to the stable bulk phase, leads to the stabilization of a wetting phase at the interfaces. Wetting and capillary condensation are here proposed as mechanisms that in membranes may serve to induce special lipid phases in between integral membrane proteins leading to long-range lipid-mediated joining forces acting between the proteins and hence providing a means of protein organization. The consequences of wetting in terms of protein aggregation and protein clustering are derived both within a simple phenomenological theory as well as within a concrete calculation on a microscopic model of lipid-protein interactions that accounts for the lipid bilayer phase equilibria and direct lipid-protein interactions governed by hydrophobic matching between the lipid bilayer hydrophobic thickness and the length of the hydrophobic membrane domain. The theoretical results are expected to be relevant for optimizing the experimental conditions required for forming protein aggregates and regular protein arrays in membranes.",
author = "Tamir Gil and Sabra, {Mads C.} and Ipsen, {John Hjort} and Mouritsen, {Ole G.}",
year = "1997",
month = "10",
doi = "10.1016/S0006-3495(97)78204-3",
language = "English",
volume = "73",
pages = "1728--1741",
journal = "Biophysical Society. Annual Meeting. Abstracts",
issn = "0523-6800",
publisher = "Biophysical Society",
number = "4",

}

RIS

TY - JOUR

T1 - Wetting and capillary condensation as means of protein organization in membranes

AU - Gil, Tamir

AU - Sabra, Mads C.

AU - Ipsen, John Hjort

AU - Mouritsen, Ole G.

PY - 1997/10

Y1 - 1997/10

N2 - Wetting and capillary condensation are thermodynamic phenomena in which the special affinity of interfaces to a thermodynamic phase, relative to the stable bulk phase, leads to the stabilization of a wetting phase at the interfaces. Wetting and capillary condensation are here proposed as mechanisms that in membranes may serve to induce special lipid phases in between integral membrane proteins leading to long-range lipid-mediated joining forces acting between the proteins and hence providing a means of protein organization. The consequences of wetting in terms of protein aggregation and protein clustering are derived both within a simple phenomenological theory as well as within a concrete calculation on a microscopic model of lipid-protein interactions that accounts for the lipid bilayer phase equilibria and direct lipid-protein interactions governed by hydrophobic matching between the lipid bilayer hydrophobic thickness and the length of the hydrophobic membrane domain. The theoretical results are expected to be relevant for optimizing the experimental conditions required for forming protein aggregates and regular protein arrays in membranes.

AB - Wetting and capillary condensation are thermodynamic phenomena in which the special affinity of interfaces to a thermodynamic phase, relative to the stable bulk phase, leads to the stabilization of a wetting phase at the interfaces. Wetting and capillary condensation are here proposed as mechanisms that in membranes may serve to induce special lipid phases in between integral membrane proteins leading to long-range lipid-mediated joining forces acting between the proteins and hence providing a means of protein organization. The consequences of wetting in terms of protein aggregation and protein clustering are derived both within a simple phenomenological theory as well as within a concrete calculation on a microscopic model of lipid-protein interactions that accounts for the lipid bilayer phase equilibria and direct lipid-protein interactions governed by hydrophobic matching between the lipid bilayer hydrophobic thickness and the length of the hydrophobic membrane domain. The theoretical results are expected to be relevant for optimizing the experimental conditions required for forming protein aggregates and regular protein arrays in membranes.

UR - http://www.scopus.com/inward/record.url?scp=0030771336&partnerID=8YFLogxK

U2 - 10.1016/S0006-3495(97)78204-3

DO - 10.1016/S0006-3495(97)78204-3

M3 - Journal article

C2 - 9336169

AN - SCOPUS:0030771336

VL - 73

SP - 1728

EP - 1741

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 4

ER -

ID: 236887163