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Journal of Chemical Physics / Volume 134 / Issue 5 / ARTICLES / Biological Molecules, Biopolymers, and Biological Systems

J. Chem. Phys. 134, 055106 (2011); http://dx.doi.org/10.1063/1.3530587 (10 pages)

Domain formation in membranes with quenched protein obstacles: Lateral heterogeneity and the connection to universality classes

T. Fischer and R. L. C. Vink

Institute of Theoretical Physics, Georg-August-Universität Göttingen, Friedrich-Hund-Platz 1, D-37077 Göttingen, Germany

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(Received 1 November 2010; accepted 2 December 2010; published online 1 February 2011)

We show that lateral fluidity in membranes containing quenched protein obstacles belongs to the universality class of the two-dimensional random-field Ising model. The main feature of this class is the absence of a phase transition: there is no critical point and macroscopic domain formation does not occur. Instead there is only one phase. This phase is highly heterogeneous with a structure consisting of microdomains. The presence of quenched protein obstacles thus provides a mechanism to stabilize lipid rafts in equilibrium. Crucial for two-dimensional random-field Ising universality is that the obstacles are randomly distributed and have a preferred affinity to one of the lipid species. When these conditions are not met standard Ising or diluted Ising universality applies. In these cases a critical point does exist which then marks the onset toward macroscopic demixing.

© 2011 American Institute of Physics

Article Outline

  1. INTRODUCTION
  2. MODEL AND METHODS
    1. Important note on the obstacle density
  3. RESULTS
    1. Pure lipid membrane: 2D Ising universality
    2. Random obstacles with preferred affinity: 2D random-field Ising universality
    3. Random obstacles without preferred affinity: Diluted 2D Ising universality
    4. Nonrandom obstacles with preferred affinity: 2D Ising universality
  4. CONCLUSION

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KEYWORDS and PACS

Keywords

biological techniques, biomembranes, Ising model, lipid bilayers, molecular biophysics, phase transformations, proteins, quenching (thermal)

PACS

ARTICLE DATA

Digital Object Identifier
http://dx.doi.org/10.1063/1.3530587

PUBLICATION DATA

ISSN

0021-9606 (print)  
1089-7690 (online)

Publisher

$abstract.society.value is a Member of CrossRef American Institute of Physics

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