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FRET in Membrane Biophysics: An Overview

Bibliographic Details
Main Author: Loura, Luís M. S.
Publication Date: 2011
Other Authors: Prieto, Manuel
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: https://hdl.handle.net/10316/110007
https://doi.org/10.3389/fphys.2011.00082
Summary: Förster resonance energy transfer (FRET), in most applications used as a "spectroscopic ruler," allows an easy determination of the donor-acceptor intermolecular distance. However, the situation becomes complex in membranes, since around each donor there is an ensemble of acceptors at non-correlated distances. In this review, state-of-the-art methodologies for this situation are presented, usually involving time-resolved data and model fitting. This powerful approach can be used to study the occurrence of phase separation ("rafts" or other type of domains), allowing their detection as well as size evaluation. Formalisms for studying lipid-protein and protein-protein interactions according to specific topologies are also addressed. The advantages and added complexity of a specific type of FRET (energy homotransfer or energy migration) are described, as well as applications of FRET under the microscope.
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spelling FRET in Membrane Biophysics: An Overviewenergy transferfluorescencelipid bilayerslipid–proteininteractionlipid raftsFörster resonance energy transfer (FRET), in most applications used as a "spectroscopic ruler," allows an easy determination of the donor-acceptor intermolecular distance. However, the situation becomes complex in membranes, since around each donor there is an ensemble of acceptors at non-correlated distances. In this review, state-of-the-art methodologies for this situation are presented, usually involving time-resolved data and model fitting. This powerful approach can be used to study the occurrence of phase separation ("rafts" or other type of domains), allowing their detection as well as size evaluation. Formalisms for studying lipid-protein and protein-protein interactions according to specific topologies are also addressed. The advantages and added complexity of a specific type of FRET (energy homotransfer or energy migration) are described, as well as applications of FRET under the microscope.Frontiers Media S.A.2011info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttps://hdl.handle.net/10316/110007https://hdl.handle.net/10316/110007https://doi.org/10.3389/fphys.2011.00082eng1664042XLoura, Luís M. S.Prieto, Manuelinfo:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2023-11-13T09:07:15Zoai:estudogeral.uc.pt:10316/110007Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T06:01:40.492425Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv FRET in Membrane Biophysics: An Overview
title FRET in Membrane Biophysics: An Overview
spellingShingle FRET in Membrane Biophysics: An Overview
Loura, Luís M. S.
energy transfer
fluorescence
lipid bilayers
lipid–proteininteraction
lipid rafts
title_short FRET in Membrane Biophysics: An Overview
title_full FRET in Membrane Biophysics: An Overview
title_fullStr FRET in Membrane Biophysics: An Overview
title_full_unstemmed FRET in Membrane Biophysics: An Overview
title_sort FRET in Membrane Biophysics: An Overview
author Loura, Luís M. S.
author_facet Loura, Luís M. S.
Prieto, Manuel
author_role author
author2 Prieto, Manuel
author2_role author
dc.contributor.author.fl_str_mv Loura, Luís M. S.
Prieto, Manuel
dc.subject.por.fl_str_mv energy transfer
fluorescence
lipid bilayers
lipid–proteininteraction
lipid rafts
topic energy transfer
fluorescence
lipid bilayers
lipid–proteininteraction
lipid rafts
description Förster resonance energy transfer (FRET), in most applications used as a "spectroscopic ruler," allows an easy determination of the donor-acceptor intermolecular distance. However, the situation becomes complex in membranes, since around each donor there is an ensemble of acceptors at non-correlated distances. In this review, state-of-the-art methodologies for this situation are presented, usually involving time-resolved data and model fitting. This powerful approach can be used to study the occurrence of phase separation ("rafts" or other type of domains), allowing their detection as well as size evaluation. Formalisms for studying lipid-protein and protein-protein interactions according to specific topologies are also addressed. The advantages and added complexity of a specific type of FRET (energy homotransfer or energy migration) are described, as well as applications of FRET under the microscope.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv https://hdl.handle.net/10316/110007
https://hdl.handle.net/10316/110007
https://doi.org/10.3389/fphys.2011.00082
url https://hdl.handle.net/10316/110007
https://doi.org/10.3389/fphys.2011.00082
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1664042X
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dc.publisher.none.fl_str_mv Frontiers Media S.A.
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instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
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