Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching

Gregory Caputo, Erwin London

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Citations (Scopus)

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

Fingerprint

Fluorescence
Membranes
Membrane Proteins
Proteins
Lipid Bilayers

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Cite this

Caputo, G., & London, E. (2013). Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching. In Lipid-Protein Interactions: Methods and Protocols (pp. 279-295). (Methods in Molecular Biology; Vol. 974). Humana Press Inc.. https://doi.org/10.1007/978-1-62703-275-9_13
Caputo, Gregory ; London, Erwin. / Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching. Lipid-Protein Interactions: Methods and Protocols. Humana Press Inc., 2013. pp. 279-295 (Methods in Molecular Biology).
@inbook{d686a8d61ebf46d1b1149389ef80e7c4,
title = "Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching",
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.",
author = "Gregory Caputo and Erwin London",
year = "2013",
month = "1",
day = "1",
doi = "10.1007/978-1-62703-275-9_13",
language = "English (US)",
isbn = "9781627032742",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "279--295",
booktitle = "Lipid-Protein Interactions",

}

Caputo, G & London, E 2013, Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching. in Lipid-Protein Interactions: Methods and Protocols. Methods in Molecular Biology, vol. 974, Humana Press Inc., pp. 279-295. https://doi.org/10.1007/978-1-62703-275-9_13

Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching. / Caputo, Gregory; London, Erwin.

Lipid-Protein Interactions: Methods and Protocols. Humana Press Inc., 2013. p. 279-295 (Methods in Molecular Biology; Vol. 974).

Research output: Chapter in Book/Report/Conference proceedingChapter

TY - CHAP

T1 - Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching

AU - Caputo, Gregory

AU - London, Erwin

PY - 2013/1/1

Y1 - 2013/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84881065878&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84881065878&partnerID=8YFLogxK

U2 - 10.1007/978-1-62703-275-9_13

DO - 10.1007/978-1-62703-275-9_13

M3 - Chapter

C2 - 23404281

AN - SCOPUS:84881065878

SN - 9781627032742

T3 - Methods in Molecular Biology

SP - 279

EP - 295

BT - Lipid-Protein Interactions

PB - Humana Press Inc.

ER -

Caputo G, London E. Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching. In Lipid-Protein Interactions: Methods and Protocols. Humana Press Inc. 2013. p. 279-295. (Methods in Molecular Biology). https://doi.org/10.1007/978-1-62703-275-9_13