The University of Southampton
University of Southampton Institutional Repository

How lipids affect the activities of integral membrane proteins

Record type: Article

The activities of integral membrane proteins are often affected by the structures of the lipid molecules that surround them in the membrane. One important parameter is the hydrophobic thickness of the lipid bilayer, defined by the lengths of the lipid fatty acyl chains. Membrane proteins are not rigid entities, and deform to ensure good hydrophobic matching to the surrounding lipid bilayer. The structure of the lipid headgroup region is likely to be important in defining the structures of those parts of a membrane protein that are located in the lipid headgroup region. A number of examples are given where the conformation of the headgroup-embedded region of a membrane protein changes during the reaction cycle of the protein; activities of such proteins might be expected to be particularly sensitive to lipid headgroup structure. Differences in hydrogen bonding potential and hydration between the headgroups of phosphatidycholines and phosphatidylethanolamines could be important factors in determining the effects of these lipids on protein activities, as well as any effects related to the tendency of the phosphatidylethanolamines to form a curved, hexagonal HII phase. Effects of lipid structure on protein aggregation and helix–helix interactions are also discussed, as well as the effects of charged lipids on ion concentrations close to the surface of the bilayer. Interpretations of lipid effects in terms of changes in protein volume, lipid free volume, and curvature frustration are also described. Finally, the role of non-annular, or ‘co-factor’ lipids, tightly bound to membrane proteins, is described.

Full text not available from this repository.

Citation

Lee, A.G. (2004) How lipids affect the activities of integral membrane proteins Biochimica et Biophysica Acta (BBA) - Biomembranes, 1666, (1-2), pp. 62-87. (doi:10.1016/j.bbamem.2004.05.012).

More information

Published date: 3 November 2004
Keywords: lipid–protein interaction, annular lipid, hydrophobic mismatch, membrane structure, membrane thickness lipid headgroup, non-annular lipid, integral membrane protein

Identifiers

Local EPrints ID: 56300
URI: http://eprints.soton.ac.uk/id/eprint/56300
ISSN: 0304-4165
PURE UUID: 524059e4-6d3b-4878-9052-d454148f65c2

Catalogue record

Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:31

Export record

Altmetrics


Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×