Journal of the American Chemical Society · 2004 · 83 citations · 9 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryStructural BiochemistryStructural BiologyCell Membrane StructureMembrane DomainsMembrane Protein TopologyMembrane ProteinsProtein StructureHelical Structure AnalysisIntegral Membrane ProteinsMembrane Protein NmrMembrane Protein Structure DeterminationNuclear Magnetic Resonance Of Membrane ProteinsPulse SequencesTransmembrane HelicesTransmembrane Proteins
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.
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Konstantin Pervushin, Roland Riek, Gerhard Wider et al. · Proceedings of the National Academy of Sciences · 1997 · 2.5K citations · Full text
Michael Salzmann, Konstantin Pervushin, Gerhard Wider et al. · Journal of the American Chemical Society · 2000 · 125 citations