The University of Southampton
University of Southampton Institutional Repository

Penetration of lipid chains into transmembrane surfaces of membrane proteins: Studies with MscL

Carney, J., East, J.M. and Lee, A.G. (2007) Penetration of lipid chains into transmembrane surfaces of membrane proteins: Studies with MscL Biophysical Journal, 92, pp. 3556-3563. (doi:10.1529/biophysj.106.102210).

Record type: Article


The transmembrane surface of a multi-helix membrane protein will be rough with cavities of various sizes between the transmembrane -helices. Efficient solvation of the surface by the lipid molecules that surround the protein in a membrane requires that the lipid fatty acyl chains be able to enter the cavities. This possibility has been investigated using fluorescence quenching methods. Trp residues have been introduced into lipid-facing sites in the first transmembrane -helix (M1) of the mechanosensitive channel of large-conductance MscL; lipid-facing residues at the N-terminal end of M1 are buried below the transmembrane surface of the protein. Fluorescence emission maxima for lipid-facing Trp residues in M1 vary with position in the bilayer comparably to those for Trp residues in the second transmembrane -helix (M2) despite the fact that lipid-facing residues in M2 are on the surface of the protein. Fluorescence emission spectra for most Trp residues on the periplasmic sides of M1 and M2 fit well to a model proposing a trough-like variation of dielectric constant across the membrane, but the relationship between location and fluorescence emission maximum on the cytoplasmic side of the membrane is more complex. The fluorescence of Trp residues in M1 is quenched efficiently by phospholipids with bromine-containing fatty acyl chains, showing that the lipid chains must be able to enter the Trp-containing cavities on the surface of MscL, resulting in efficient solvation of the surface.

Full text not available from this repository.

More information

Published date: 1 May 2007


Local EPrints ID: 56404
ISSN: 0006-3495
PURE UUID: c6e357cd-98bc-4138-b1d6-01903f09174d

Catalogue record

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

Export record



Author: J. Carney
Author: J.M. East
Author: A.G. Lee

University divisions

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 supports OAI 2.0 with a base URL of

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.