Fluorescence quenching methods to study lipid-protein interactions

Carney, Joanne, East, J. Malcolm, Mall, Sanjay, Marius, Phedra, Powl, Andrew M., Wright, J. Neville and Lee, Anthony G. 2006. Fluorescence quenching methods to study lipid-protein interactions. Current Protocols in Protein Science 45 (1) , 19.12.1-19.12.17. 10.1002/0471142301.ps1912s45

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Abstract

This unit describes how fluorescence quenching methods can be used to determine binding constants for phospholipids binding to intrinsic membrane proteins. Reconstitution of a Trp‐containing intrinsic membrane protein with bromine‐containing phospholipids leads to quenching of the Trp fluorescence of the protein; the extent of quenching depends on the strength of binding of the phospholipid to the protein. Protocols are included for the synthesis of bromine‐containing phospholipids from phospholipids containing carbon‐carbon double bonds in their fatty acyl chains and for the reconstitution of membrane proteins into bilayers containing bromine‐containing phospholipids. Details are included on data analysis, including equations and software that can be used for fitting the fluorescence quenching data.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine Centre for Trials Research (CNTRR)
Publisher:	Wiley
Last Modified:	24 Apr 2019 11:00
URI:	https://orca.cardiff.ac.uk/id/eprint/121348

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