title: Construction of covalent membrane protein complexes and high-throughput selection of membrane mimics.
abstract: The association of transmembrane (TM) helices underlies membrane protein structure and folding. Structural studies of TM complexes are limited by complex stability and the often time-consuming selection of suitable membrane mimics. Here, methodology for the efficient, preparative scale construction of covalent TM complexes and the concomitant high-throughput selection of membrane mimics is introduced. For the employed integrin αIIbβ3 model system, the methodology identified phospholipid bicelles, including their specific composition, as the best membrane mimic. The method facilitates structure determination by NMR spectroscopy as exemplified by the measurement of previously inaccessible residual dipolar couplings and (15)N relaxation parameters.
authors.affiliation: Department of Biochemistry & Molecular Biology, Keck School of Medicine, University of Southern California, Los Angeles, California 90033, United States.
authors.forename: Jae-Eun
authors.initials: JE
authors.lastname: Suk
authors.forename: Alan J
authors.initials: AJ
authors.lastname: Situ
authors.forename: Tobias S
authors.initials: TS
authors.lastname: Ulmer
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010743:Phospholipids / Q000737:chemistry*; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D010743:Phospholipids; D019039:Platelet Glycoprotein GPIIb-IIIa Complex