Orientation and dynamics of transmembrane peptides: the power of simple models.

Orientation and dynamics of transmembrane peptides: the power of simple models.
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DOI:
10.1007/s00249-009-0567-1
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发表时间:
2010-03
影响因子:
2
通讯作者:
Killian, J. Antoinette
Killian, J. Antoinette
中科院分区:
生物学4区
文献类型:
--
作者:
Holt, Andrea;Killian, J. Antoinette

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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.
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