title: Phage-induced alignment of membrane proteins enables the measurement and structural analysis of residual dipolar couplings with dipolar waves and lambda-maps.
abstract: At pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide gel alignment, Dipolar Waves can be used to directly assess the secondary structure and a lambda-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0307, USA.
authors.forename: Sang Ho
authors.initials: SH
authors.lastname: Park
authors.forename: Woo Sung
authors.initials: WS
authors.lastname: Son
authors.forename: Rishi
authors.initials: R
authors.lastname: Mukhopadhyay
authors.forename: Homayoun
authors.initials: H
authors.lastname: Valafar
authors.forename: Stanley J
authors.initials: SJ
authors.lastname: Opella
mesh_terms: D000180:Acrylic Resins / Q000737:chemistry; D017104:Bacteriophage M13 / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010743:Phospholipids / Q000737:chemistry; D017433:Protein Structure, Secondary
chemical_list: D000180:Acrylic Resins; D008565:Membrane Proteins; D010743:Phospholipids; C016680:polyacrylamide gels