Bilayer Hydrophobic Thickness and Integral Membrane Protein Function

Title: Bilayer Hydrophobic Thickness and Integral Membrane Protein Function

Volume: 12 Issue: 8

Author(s): Larisa E. Cybulski and Diego de Mendoza

Affiliation:

Keywords: Membrane thickness, hydrophobic mismatch, transmembrane protein, transmembrane peptide, hydrophobic amino acids, hydrophobic helices, HIV, TM1

Abstract: The influence of the lipid environment on the function of membrane proteins is increasingly recognized as crucial. Nevertheless, the molecular mechanisms underlying protein-lipid interactions remain obscure. Membrane lipid composition has a regulatory effect on membrane protein activity, and for a number of membrane proteins a clear correlation was found between protein activity and properties of the membrane bilayer such as fluidity. Membrane thickness is an important property of a lipid bilayer. It is expected that hydrophobic thickness match the hydrophobic thickness of transmembrane segments of integral membrane proteins. Any mismatch between the hydrophobic thicknesses of the lipid bilayer and the protein would lead to some modification in either the structure of the protein or the structure of the bilayer, or both. Consequent rearrangements may result in changes in protein activity. Here we review the behavior of several transmembrane proteins whose activity is altered by hydrophobic core thickness.

Cite this article as:

E. Cybulski Larisa and de Mendoza Diego, Bilayer Hydrophobic Thickness and Integral Membrane Protein Function, Current Protein & Peptide Science 2011; 12 (8) . https://dx.doi.org/10.2174/138920311798841681