Bilayer thickness and membrane protein function: an energetic perspective.

  title={Bilayer thickness and membrane protein function: an energetic perspective.},
  author={Olaf S. Andersen and Roger E. Koeppe},
  journal={Annual review of biophysics and biomolecular structure},
  • O. AndersenR. Koeppe
  • Published 3 May 2007
  • Biology, Chemistry
  • Annual review of biophysics and biomolecular structure
The lipid bilayer component of biological membranes is important for the distribution, organization, and function of bilayer-spanning proteins. This regulation is due to both specific lipid-protein interactions and general bilayer-protein interactions, which modulate the energetics and kinetics of protein conformational transitions, as well as the protein distribution between different membrane compartments. The bilayer regulation of membrane protein function arises from the hydrophobic… 

Protein–Lipid Interactions in Biological Membranes

Examples of recent advances in electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopy revealing structural and orientational information about integral membrane protein in fluid lipid bilayers are presented and a continuum elastic description of protein–lipid interactions is presented with emphasis on how to quantify the energetics of protein-lipid interaction.

Mechanochemical coupling of lipid organization and protein function through membrane thickness deformations.

The resulting lipid-protein organization can endow membrane proteins with diverse and controlled mechanical environments that, via protein-induced lipid bilayer thickness deformations, can strongly influence protein function.

Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes

An introduction to the regulation of membrane protein function by the bilayer physical properties is provided and the use of gramicidin channels as molecular force probes for studying this mechanism is described, with a unique ability to discriminate between consequences of changes in monolayer curvature and bilayer elastic moduli.

Bilayer-thickness-mediated interactions between integral membrane proteins.

The work presented here puts into place an analytic and numerical framework which allows calculation of bilayer-mediated elastic interactions between integral membrane proteins for the complicated protein shapes suggested by structural biology and at the small protein separations most relevant for the crowded membrane environments provided by living cells.

Curvature forces in membrane lipid-protein interactions.

An increased awareness of curvature forces suggests that research will accelerate as structural biology becomes more closely entwined with the physical chemistry of lipids in explaining membrane structure and function.

Curvature Forces in Membrane Lipid − Protein Interactions

This review describes how conformational changes in membrane proteins, involving folding, stability, and membrane shape transitions, potentially involve elastic remodeling of the lipid bilayer.

Regulation of membrane proteins through local heterogeneity in lipid bilayer thickness.

It is suggested that protein-induced lipid bilayer thickness deformations endow proteins in cell membranes with diverse and controlled mechanical environments that, in turn, allow targeted regulation of membrane proteins.

Soft Matter in Lipid-Protein Interactions.

This review considers hydrophobic matching of the intramembranous proteolipid boundary to explain the conformational changes and oligomeric states of proteins within the bilayer.

Membrane Lipid-Protein Interactions

Curvature elasticity and hydrophobicity of native lipid mixtures play key roles in functional proteolipid couplings and give insights into protein activation mechanisms in cellular membranes.



Regulation of Sodium Channel Function by Bilayer Elasticity

Whether voltage-dependent skeletal-muscle sodium channels, expressed in HEK293 cells, are regulated by bilayer elasticity, as monitored using gramicidin A (gA) channels is examined, providing strong support for the notion that bilayer–protein hydrophobic coupling allows the bilayers elastic properties to regulate membrane protein function.

Regulation of membrane protein function by lipid bilayer elasticity—a single molecule technology to measure the bilayer properties experienced by an embedded protein

  • J. A. Lundbæk
  • Biology
    Journal of physics. Condensed matter : an Institute of Physics journal
  • 2006
The present review summarizes studies which have demonstrated that the hydrophobic interactions between a membrane protein and the host lipid bilayer provide an energetic coupling, whereby protein function can be regulated by the bilayer elasticity.

Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels.

It is shown that alterations in curvature stress, due to alterations in the electrostatic energy of dioleoylphosphatidylserine bilayers, modulate the structurally well-defined gramicidin A monomer <--> dimer reaction and provides further evidence for the importance of mechanical interactions between a bilayer and its imbedded proteins for protein structure and function.

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  • Biology, Chemistry
    Biochimica et biophysica acta
  • 1998

Lipid-protein interactions in biological membranes: a structural perspective.

  • A. Lee
  • Biology
    Biochimica et biophysica acta
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A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch.

Roles of bilayer material properties in function and distribution of membrane proteins.

Theoretical and experimental studies show that the binding of either cytoplasmic proteins or extracellular peptides to membranes is regulated by the presence of charged lipids and that the sorting of transmembrane proteins into or out of membrane microdomains (rafts) depends on several factors, including bilayer material properties governed by the existence of cholesterol.

How lipids affect the activities of integral membrane proteins.