A theoretical study of lipid-protein interactions in bilayers

Biophys J. 1983 Jun;42(3):219-24. doi: 10.1016/S0006-3495(83)84389-6.

Abstract

We present a theoretical study of the effect of different types of lipid-protein interactions on the thermodynamic properties of protein-containing lipid bilayers. The basis of this work is a theoretical model for pure lipid bilayer phase transitions developed earlier by Scott. Simple assumptions on the nature of the lipid conformations near a protein strongly affect the predicted properties of the model. Here we consider (a) random protein-lipid contacts, (b) enhanced contact between protein and lipid with a number of gauche bonds, and (c) enhanced contact between protein and all-trans but tilted lipid chains. Comparison of predicted results with experimental data seems to favor point c above but, by itself point c does not work well at larger protein concentrations. The results are discussed in the light of spectroscopic data, lipid-protein (plus annular lipid) miscibility, and interprotein forces.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Lipid Bilayers*
  • Mathematics
  • Models, Biological
  • Molecular Conformation
  • Protein Binding
  • Protein Conformation
  • Proteins*
  • Thermodynamics

Substances

  • Lipid Bilayers
  • Proteins