title: NMR assignments for a helical 40 kDa membrane protein.
abstract: Backbone nuclear magnetic resonance (NMR) assignments were achieved for diacylglycerol kinase (DAGK) in detergent micelles. DAGK is a homotrimeric integral membrane protein comprised of 121 residue subunits, each having three transmembrane segments. Assignments were made using TROSY-based pulse sequences. DAGK was found to be an almost exclusively helical protein. This work points to the feasibility of both solving the structure of DAGK using solution NMR methods and using NMR as a primary tool in structural studies of other helical integral membrane proteins of similar size and complexity.
authors.affiliation: Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725, USA.
authors.forename: Kirill
authors.initials: K
authors.lastname: Oxenoid
authors.forename: Hak Jun
authors.initials: HJ
authors.lastname: Kim
authors.forename: Jaison
authors.initials: J
authors.lastname: Jacob
authors.forename: Frank D
authors.initials: FD
authors.lastname: Sönnichsen
authors.forename: Charles R
authors.initials: CR
authors.lastname: Sanders
mesh_terms: D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D019852:Diacylglycerol Kinase / Q000737:chemistry*; D004926:Escherichia coli; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000577:Amides; D008565:Membrane Proteins; D019852:Diacylglycerol Kinase