Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Penetration of lipid chains into the transmembrane surface of TbMscL

Carney, Joanne, East, J. Malcolm and Lee, Anthony G. 2007. Penetration of lipid chains into the transmembrane surface of TbMscL. Biophysical Journal 92 , pp. 3556-3563. 10.1529/biophysj.106.102210

Full text not available from this repository.

Abstract

The transmembrane surface of a multi-helix membrane protein will be rough with cavities of various sizes between the transmembrane α-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 α-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 α-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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Centre for Trials Research (CNTRR)
Medicine
Publisher: Biophysical Society
ISSN: 0006-3495
Last Modified: 24 Apr 2019 10:52
URI: http://orca.cf.ac.uk/id/eprint/121346

Citation Data

Cited 13 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item