| Literature DB >> 25086504 |
Signe Mathiasen1, Sune M Christensen1, Juan José Fung2, Søren G F Rasmussen3, Jonathan F Fay4, Sune K Jorgensen1, Salome Veshaguri1, David L Farrens4, Maria Kiskowski5, Brian Kobilka6, Dimitrios Stamou1.
Abstract
Proteoliposome reconstitution is a standard method to stabilize purified transmembrane proteins in membranes for structural and functional assays. Here we quantified intrareconstitution heterogeneities in single proteoliposomes using fluorescence microscopy. Our results suggest that compositional heterogeneities can severely skew ensemble-average proteoliposome measurements but also enable ultraminiaturized high-content screens. We took advantage of this screening capability to map the oligomerization energy of the β2-adrenergic receptor using ∼10(9)-fold less protein than conventional assays.Entities:
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Year: 2014 PMID: 25086504 PMCID: PMC4485457 DOI: 10.1038/nmeth.3062
Source DB: PubMed Journal: Nat Methods ISSN: 1548-7091 Impact factor: 28.547