FRET in Membrane Biophysics: An Overview
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
Texto Completo: | https://hdl.handle.net/10316/110007 https://doi.org/10.3389/fphys.2011.00082 |
Resumo: | 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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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 |
format |
article |
status_str |
publishedVersion |
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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Frontiers Media S.A. |
publisher.none.fl_str_mv |
Frontiers Media S.A. |
dc.source.none.fl_str_mv |
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FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
collection |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
repository.name.fl_str_mv |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia |
repository.mail.fl_str_mv |
info@rcaap.pt |
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1833602552754601984 |