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Lateral Pressure Profile, Spontaneous Curvature Frustration, and the Incorporation and Conformation of Proteins in Membranes

Max-Planck-Institut für biophysikalische Chemie, Abt. Spektroskopie, Göttingen, Germany

Correspondence: Address reprint requests to D. Marsh, Tel.: 49-551-201-1285; E-mail: dmarsh{at}gwdg.de.

Lipid-protein interactions are an important determinant of the stability and function of integral and transmembrane proteins. In addition to local interactions at the lipid-protein interface, global interactions such as the distribution of internal lateral pressure may also influence protein conformation. It is shown here that the effects of the membrane lateral pressure profile on the conformation or insertion of proteins in membranes are equivalent to the elastic response to the frustrated spontaneous curvature, c_o, of the component lipid monolayer leaflets. The chemical potential of the protein in the membrane is predicted to depend linearly on the spontaneous curvature of the lipid leaflets, just as does the contribution of the protein to the elastic bending energy of the lipid, and to be independent of the hydrophobic tension, _phob, at the lipid-water interface. Analysis of the dependence of protein partitioning or conformational transitions on spontaneous curvature of the constituent lipids gives an experimental estimate for the cross-sectional intramembrane shape of the protein or its difference between conformations. Values in the region of 50–110 Ų are estimated for the effective cross-sectional shape changes on the insertion and conductance transitions of alamethicin, and on the activation of CTP:phosphocholine cytidylyltransferase or rhodopsin in lipid membranes. Much larger values are estimated for the mechanosensitive channel, MscL. Values for the change in intramembrane shape may also be used, together with determinations of lipid relative association constants, to estimate contributions of direct lipid-protein interactions to the lateral pressure experienced by the protein. Changes in chemical potential 12 kJ mol^–1 can be estimated for radial changes of 1 Å in a protein of diameter 40 Å.

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