Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 40, Pages 16628-16633Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1103742108
Keywords
mattress model; membrane domain; protein-lipid interaction; self-assembly; annular lipid
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Funding
- Academy of Finland
- Deutsche Forschungsgemeinschaft (DFG) [Schwerpunktprogramm1175, SI459/2-1, Transregio 83, TRR83 TP02]
- Bundesministerium fur Bildung und Forschung [03FO1212]
- European Science Foundation [SI459/3-1]
- Klaus Tschira Foundation
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Theoretical studies predict hydrophobic matching between transmembrane domains of proteins and bilayer lipids to be a physical mechanism by which membranes laterally self-organize. We now experimentally study the direct consequences of mismatching of transmembrane peptides of different length with bilayers of different thicknesses at the molecular level. In both model membranes and simulations we show that cholesterol critically constrains structural adaptations at the peptide-lipid interface under mismatch. These constraints translate into a sorting potential and lead to selective lateral segregation of peptides and lipids according to their hydrophobic length.
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