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dc.contributor.author
Antollini, Silvia Susana  
dc.contributor.author
Barrantes, Francisco Jose  
dc.contributor.other
Dopico, Alex M  
dc.date.available
2020-06-19T20:20:11Z  
dc.date.issued
2007  
dc.identifier.citation
Antollini, Silvia Susana; Barrantes, Francisco Jose; Laurdan Studies of Membrane Lipid-Acetylcholine Receptor Protein Interactions; Humana Press; 400; 2007; 531-542  
dc.identifier.isbn
978-1-58829-662-7  
dc.identifier.uri
http://hdl.handle.net/11336/107761  
dc.description.abstract
The extrinsic fluorescent probe Laurdan (6-dodecanoyl-2-dimethylamino naphthalene) exhibits extreme sensitivity to the polarity and to the molecular dynamics of the dipoles in its environment. Dipolar relaxation processes are reflected as relatively large spectral shifts. Steady-state measurements of the so-called general polarization (GP) of Laurdan exploit the advantageous spectral properties of Laurdan. Since the main solvent dipoles surrounding Laurdan in biological membranes are water molecules, when no relaxation occurs GP values are high, indicating low water content in the hydrophilic/hydrophobic interface region. Laurdan fluorescence can also be used to obtain topographical information. A hitherto unexploited property of Laurdan, namely its ability to act as a Förster-type resonance energy transfer (FRET) acceptor of tryptophan emission, was used to learn about the physical state of lipids within Förster distance from donor tryptophan residues in integral membrane proteins. The application of this technique to the paradigm integral membrane protein, the nicotinic acetylcholine receptor, is described in this chapter.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Humana Press  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
CHOLINERGIC RECEPTOR  
dc.subject
FLUORESCENCE SPECTROSCOPY  
dc.subject
FÖRSTER RESONANCE ENERGY TRANSFER  
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LAURDAN  
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INTRINSIC FLUORESCENCE  
dc.subject.classification
Biofísica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Laurdan Studies of Membrane Lipid-Acetylcholine Receptor Protein Interactions  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.type
info:eu-repo/semantics/bookPart  
dc.type
info:ar-repo/semantics/parte de libro  
dc.date.updated
2020-05-27T18:01:39Z  
dc.journal.volume
400  
dc.journal.pagination
531-542  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Nueva Jersey  
dc.description.fil
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina  
dc.description.fil
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/protocol/10.1007%2F978-1-59745-519-0_36  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/978-1-59745-519-0_36  
dc.conicet.paginas
621  
dc.source.titulo
Methods in Molecular Biology