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Wetting and Capillary Condensation as Means of Protein Organization in Membranes

Authors
Publisher
Biophysical Society
Publication Date
Keywords
  • Wetting And Capillary Condensation Are Thermodynamic Phenomena In Which The Special Affinity Of Inte
  • 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 In
  • The Consequences Of Wetting In Terms Of Protein Aggregation And Protein Clustering Are Derived Both
  • The Theoretical Results Are Expected To Be Relevant For Optimizing The Experimental Conditions Requi
Disciplines
  • Biology
  • Philosophy
  • Physics

Abstract

Wetting and Capillary Condensation as Means of Protein Organization in Membranes - DTU Orbit (25/04/14) Wetting and Capillary Condensation as Means of Protein Organization in Membranes - DTU Orbit (25/04/14) Wetting and Capillary Condensation as Means of Protein Organization in Membranes 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. General information State: Published Organisations: Department of Chemistry Authors: Gil, T. (Intern), Sabra, M. C. (Intern), Ipsen, J. H. (Intern), Mouritsen, O. G. (Intern) Pages: 1728-1741 Publication date: 1997 Main Research Area: Technical/natural sciences Publication information Journal: Biophysical Journal Volume: 73 Journal number: 4 ISSN (Print): 0006-3495 Ratings: FI (2012): 1 ISI indexed (2012): yes FI (2011): 1 ISI indexed (2011): yes FI (2010): 1 FI (2009): 1 FI (2008): 2 Original language: English Source: orbit Source-ID: 168786 Publicatio

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