Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli

Membrane proteins are usually solubilized in polar solvents by incorporation into micelles. Even for small membrane proteins these mixed micelles have rather large molecular masses, typically beyond 50 000 Da. The NMR technique TROSY (transverse relaxation-optimized spectroscopy) has been developed...

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Veröffentlicht in:	FEBS Letters 2001-08, Vol.504 (3), p.173-178
Hauptverfasser:	Fernández, César, Hilty, Christian, Bonjour, Sophie, Adeishvili, Koba, Pervushin, Konstantin, Wüthrich, Kurt
Format:	Artikel
Sprache:	eng
Schlagworte:	2D, two-dimensional 3D, three-dimensional Bacterial Outer Membrane Proteins - chemistry Cell Membrane - chemistry COSY, correlation spectroscopy DHPC, dihexanoylphosphatidylcholine (1,2-dihexanoyl-sn-glycero-3-phosphocholine) DPC, dodecylphosphocholine Escherichia coli - chemistry Escherichia coli Proteins Hydrolases Isotope labeling Magnetic Resonance Spectroscopy - methods Membrane protein Models, Molecular NMR structure NOE, nuclear Overhauser effect NOESY, NOE spectroscopy OmpA, outer membrane protein A from E. coli OmpX, outer membrane protein X from E. coli Outer membrane protein A from E. coli Outer membrane protein X from E. coli ppm, parts per million Transverse relaxation-optimized spectroscopy TROSY, transverse relaxation-optimized spectroscopy
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