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A FlAsH–Tetracysteine Assay for Quantifying the Association and Orientation of Transmembrane α‐Helices
Author(s) -
Pace Christopher J.,
Huang Qiongying,
Wang Fang,
Palla Kanwal S.,
Fuller Amelia A.,
Gao Jianmin
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000736
Subject(s) - antiparallel (mathematics) , flash (photography) , association (psychology) , computational biology , transmembrane protein , chemistry , biophysics , computer science , biochemistry , biology , physics , philosophy , receptor , epistemology , optics , quantum mechanics , magnetic field
Lighting up protein dimers in membranes: The association of membrane proteins plays a critical role in biology. We describe a FlAsH–tetracysteine (tC) assay that detects protein dimerization in lipid bilayers with a fluorescent readout. The stringent spatial requirement of FlAsH–tC complex formation readily differentiates helix dimers in parallel and antiparallel orientations.