Quantification of protein-protein interactions within membranes by fluorescence correlation spectroscopy

The characterization of interactions between membrane proteins as they take place within the lipid bilayer poses a technical challenge, which is currently very difficult and, in many cases, impossible to overcome. The recent development of a method based in the combination two-color fluorescence cro...

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Bibliographic Details
Main Authors: Bleicken, Stephanie (Author) , Otsuki, Miki (Author) , García-Sáez, Ana J. (Author)
Format: Article (Journal)
Language:English
Published: 2011
In: Current protein & peptide science
Year: 2011, Volume: 12, Issue: 8, Pages: 691-698
ISSN:1875-5550
Online Access:Verlag, lizenzpflichtig, Volltext: https://www.eurekaselect.com/article/34211
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Author Notes:Stephanie Bleicken, Miki Otsuki, and Ana J. Garcia-Saez
Description
Summary:The characterization of interactions between membrane proteins as they take place within the lipid bilayer poses a technical challenge, which is currently very difficult and, in many cases, impossible to overcome. The recent development of a method based in the combination two-color fluorescence cross-correlation spectroscopy with scanning of the focal volume allows the detection and quantification of interactions between biomolecules inserted in biological membranes. This powerful strategy has allowed the quantitative analysis of diverse systems, such as the association between proteins of the Bcl-2 family involved in apoptosis regulation or the binding between a growth factor and its receptor during signaling. Here, we review the last developments to quantify protein/protein interactions in lipid membranes and focus on the use of fluorescence-correlation-spectroscopy approaches for that purpose.
Item Description:Gesehen am 30.03.2022
Physical Description:Online Resource
ISSN:1875-5550