Modulation of membrane structure and function by hydrophobic mismatch between proteins and lipids
by Killian, Josephine Antoinette; De Planque, Maurits R. R.; Van der Wel, Patrick C. A.; Salemink, Irene; De Kruijff, Ben; Greathouse, Denise V.; Koeppe II, R. Erdman
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.
- Pure and Applied Chemistry
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