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How lipids and proteins interact in a membrane: a molecular approach

How lipids and proteins interact in a membrane: a molecular approach
How lipids and proteins interact in a membrane: a molecular approach
Membrane proteins in a biological membrane are surrounded by a shell or annulus of ‘solvent’ lipid molecules. These lipid molecules in general interact rather non-specifically with the protein molecules, although a few ‘hot-spots’ may be present on the protein where anionic lipids bind with high affinity. Because of the low structural specificity of most of the annular sites, the composition of the lipid annulus will be rather similar to the bulk lipid composition of the membrane. The structures of the solvent lipid molecules are important in determining the conformational state of a membrane protein, and hence its activity, through charge and hydrogen bonding interactions between the lipid headgroups and residues in the protein, and through hydrophobic matching between the protein and the surrounding lipid bilayer. Evidence is also accumulating for the presence of ‘co-factor’ lipid molecules binding with high specificity to membrane proteins, often between transmembrane a-helices, and often being essential for activity.
1742-2051
203-212
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e

Lee, A.G. (2005) How lipids and proteins interact in a membrane: a molecular approach. Molecular BioSystems, 1, 203-212. (doi:10.1039/b504527d).

Record type: Article

Abstract

Membrane proteins in a biological membrane are surrounded by a shell or annulus of ‘solvent’ lipid molecules. These lipid molecules in general interact rather non-specifically with the protein molecules, although a few ‘hot-spots’ may be present on the protein where anionic lipids bind with high affinity. Because of the low structural specificity of most of the annular sites, the composition of the lipid annulus will be rather similar to the bulk lipid composition of the membrane. The structures of the solvent lipid molecules are important in determining the conformational state of a membrane protein, and hence its activity, through charge and hydrogen bonding interactions between the lipid headgroups and residues in the protein, and through hydrophobic matching between the protein and the surrounding lipid bilayer. Evidence is also accumulating for the presence of ‘co-factor’ lipid molecules binding with high specificity to membrane proteins, often between transmembrane a-helices, and often being essential for activity.

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More information

Published date: 1 September 2005

Identifiers

Local EPrints ID: 56201
URI: https://eprints.soton.ac.uk/id/eprint/56201
ISSN: 1742-2051
PURE UUID: 4c0cc044-0a87-4ba7-b42c-8a2e75fc79e6

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Date deposited: 06 Aug 2008
Last modified: 13 Mar 2019 20:35

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