Resolution of complex fluorescence spectra of lipids and nicotinic acetylcholine receptor by multivariate analysis reveals protein-mediated effects on the receptor's immediate lipid microenvironment

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dc.creatorWenz, Jorge J
dc.creatorBarrantes, Francisco J
dc.date2009-02-18
dc.date.accessioned2026-07-07T12:43:32Z
dc.date.available2026-07-07T12:43:32Z
dc.descriptionAnalysis of fluorescent spectra from complex biological systems containing various fluorescent probes with overlapping emission bands is a challenging task. Valuable information can be extracted from the full spectra, however, by using multivariate analysis (MA) of measurements at different wavelengths. We applied MA to spectral data of purified Torpedo nicotinic acetylcholine receptor (AChR) protein reconstituted into liposomes made up of dioleoylphosphatidic acid (DOPA) and dioleoylphosphatidylcholine (DOPC) doped with two extrinsic fluorescent probes (NBD-cholesterol/pyrene-PC). Forster resonance energy transfer (FRET) was observed between the protein and pyrene-PC and between pyrene-PC and NBD-cholesterol, leading to overlapping emission bands. Partial least squares analysis was applied to ...
dc.description17 pages, 5 figures
dc.identifierhttps://arxiv.org/abs/0902.3120
dc.identifierhttp://arxiv.org/abs/0902.3120
dc.identifierPMC Biophysics 2008, 1:6
dc.identifierdoi:10.1186/1757-5036-1-6
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/220453
dc.subjectBiological Physics
dc.titleResolution of complex fluorescence spectra of lipids and nicotinic acetylcholine receptor by multivariate analysis reveals protein-mediated effects on the receptor's immediate lipid microenvironment
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