Modulation of membrane structure and function by hydrophobic mismatch between proteins and lipids
by Killian, J. A.; de Planque, M. R. R.; van der Wel, P. C. A.; Salemink, I.; de Kruijff, B.; Greathouse, D. V.; Koeppe, R. E.
The structure and function of biological membranes can be expected to be sensitive to the extent of hydrophobic matching between the length of the membrane-spanning part of intrinsic membrane proteins and the hydrophobic thickness of the lipid bilayer. To gain insight into the consequences of hydrophobic mismatch on a molecular level, we have carried out systematic studies on well-defined peptide/lipid complexes, using artifical transmembrane peptides, anchored to the membrane by tryptophan residues. It is shown that hydrophobic mismatch can result in a dramatic change in lipid organization, and that the presence of interfacially localized aromatic amino acid residues is important for determining the exact consequences of hydrophobic mismatch.