Homodimerization of amyloid precursor protein at the plasma membrane: a homoFRET study by time-resolved fluorescence anisotropy imaging.

Homodimerization of amyloid precursor protein at the plasma membrane: a homoFRET study by time-resolved fluorescence anisotropy imaging.

Classical FRET (Förster Resonance Energy Transfer) using two fluorescent labels (one for the donor and another one for the acceptor) is not efficient for studying the homodimerization of a protein as only half of the homodimers formed can be identified by this technique. We thus resorted to homoFRET...

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Bibliographic Details
Main Authors: Viviane Devauges, Catherine Marquer, Sandrine Lécart, Jack-Christophe Cossec, Marie-Claude Potier, Emmanuel Fort, Klaus Suhling, Sandrine Lévêque-Fort
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3433432?pdf=render

Internet

http://europepmc.org/articles/PMC3433432?pdf=render

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