Molecular theory of hydrophobic mismatch between lipids and peptides

Details Molecular theory of hydrophobic mismatch between lipids and peptides Molecular theory of hydrophobic mismatch between lipids and peptides

2001-08-14

arxiv.org/abs/cond-mat/0108237v1

Physics

Condensed Matter

Soft Condensed Matter

14 pages, 5 figures

Scientific paper

10.1063/1.1477927

Effects of the mismatch between the hydrophobic length, d, of transmembrane alpha helices of integral proteins and the hydrophobic thickness, D_h, of the membranes they span are studied theoretically utilizing a microscopic model of lipids. In particular, we examine the dependence of the period of a lamellar phase on the hydrophobic length and volume fraction of a rigid, integral, peptide. We find that the period decreases when a short peptide, such that dD_h, is inserted. The effect is due to the replacement of extensible lipid tails by rigid peptide. As the peptide length is increased, the lamellar period continues to increase, but at a slower rate, and can eventually decrease. The amount of peptide which fails to incorporate and span the membrane increases with the magnitude of the hydrophobic mismatch |d-D_h|. We explicate these behaviors which are all in accord with experiment. Predictions are made for the dependence of the tilt of a single trans-membrane alpha helix on hydrophobic mismatch and helix density.

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