Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching

Gregory Caputo, Erwin London

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Scopus citations

Abstract

The location of fluorescent groups relative to the lipid bilayer can be evaluated using fluorescence quenchers embedded in the membrane and/or dissolved in aqueous solution. Quenching can be used to define the membrane topography of membrane proteins and individual membrane-embedded hydrophobic helices by combining it with the placement of fluorescent groups, including Trp, at defined sequence positions. This chapter briefly discusses various quenching methods for studies of membrane protein topography and provides detailed protocols for dual quencher analysis, a rapid, highly sensitive, and experimentally flexible approach in which the information gained from both a membrane-embedded and aqueous quencher is combined.

Original languageEnglish (US)
Title of host publicationLipid-Protein Interactions
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Pages279-295
Number of pages17
ISBN (Print)9781627032742
DOIs
StatePublished - Jan 1 2013

Publication series

NameMethods in Molecular Biology
Volume974
ISSN (Print)1064-3745

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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