TITLE

Bilayer Hydrophobic Thickness and Integral Membrane Protein Function

AUTHOR(S)
Cybulski, Larisa E.; de Mendoza, Diego
PUB. DATE
December 2011
SOURCE
Current Protein & Peptide Science;Dec2011, Vol. 12 Issue 8, p760
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
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.
ACCESSION #
70350097

 

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