Abstract
In this review we discuss recent insights obtained from well-characterized model systems into the factors that determine the orientation and tilt angles of
transmembrane peptides in lipid bilayers. We will compare tilt angles of synthetic peptides with those of natural peptides and proteins, and we will discuss how tilt can be
modulated by hydrophobic mismatch between the thickness of the bilayer and the length of the membrane spanning part of the peptide or protein. In particular, we will
focus on results obtained on tryptophan-flanked model peptides (WALP peptides) as a case study to illustrate possible consequences of hydrophobic mismatch in
molecular detail and to highlight the importance of peptide dynamics for the experimental determination of tilt angles.
We will conclude with discussing some future prospects and challenges concerning the use of simple peptide/lipid model systems as a tool to understand membrane structure
and function.
Original language | English |
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Pages (from-to) | 609-621 |
Number of pages | 13 |
Journal | European Biophysics Journal |
Volume | 39 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2010 |