Ontology highlight
ABSTRACT:
SUBMITTER: Felce JH
PROVIDER: S-EPMC4070276 | biostudies-other | 2014 Jun
REPOSITORIES: biostudies-other
Biophysical journal 20140601 12
We show that in conventional, competition-based bioluminescence resonance energy transfer (BRET) assays of membrane protein stoichiometry, the presence of competitors can alter tagged-protein density and artifactually reduce energy transfer efficiency. A well-characterized monomeric type I membrane protein, CD86, and two G protein-coupled receptors β2AR and mCannR2, all of which behave as dimers in these conventional assays, exhibit monomeric behavior in an improved competition-based type-3 BRET ...[more]