Membrane alignment of the pore-forming component TatAd of the twin-arginine translocase from bacillus subtilis resolved by solid-state NMR spectroscopy

Journal of the American Chemical Society

Volumn 132, Issue 45, 2010, Pages 15945-15956

  Walther, Torsten H ^a   Grage, Stephan L ^a   Roth, Nadine ^a   Ulrich, Anne S ^a  

^a KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPHILICS; AZIMUTHAL ROTATION; BACILLUS SUBTILIS; BACTERIAL MEMBRANES; BICELLES; DIPOLAR COUPLINGS; FOLDED PROTEINS; HELICAL CHARACTER; LABELED PROTEINS; LIQUID STATE; MEMBRANE-BOUND; NMR STUDIES; PLANT CHLOROPLASTS; SIDE CHAINS; SOLID STATE NMR; SOLID-STATE NMR SPECTROSCOPY; TILT ANGLE; TRANSLOCASES; TRANSMEMBRANE SEGMENTS; TRANSMEMBRANES; TWIN-ARGININE TRANSLOCASE (TAT);

ALIGNMENT; AMINO ACIDS; BACTERIOLOGY; LIPID BILAYERS; MEMBRANES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID STATE PHYSICS; WHEELS;

PROTEINS;

AMPHOPHILE; ARGININE TRANSLOCASE; CARRIER PROTEIN; LIPID; MEMBRANE PROTEIN; NITROGEN 15; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BACILLUS SUBTILIS; BACTERIAL MEMBRANE; CHANNEL GATING; CROSS COUPLING REACTION; LIPID BILAYER; MEMBRANE BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POROSITY; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SOLID STATE;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CELL MEMBRANE; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; POROSITY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

EID: 78449242888     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja106963s     Document Type: Article

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