Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Solid-state Magic-Angle Spinning NMR of Outer-Membrane Protein G from Escherichia Coli.

MPG-Autoren
/persons/resource/persons137930

Vinothkumar,  Kutta Ragunath
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137764

Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Hiller, M., Krabben, L., Vinothkumar, K. R., Castellani, F., van Rossum, B.-J., Kühlbrandt, W., et al. (2005). Solid-state Magic-Angle Spinning NMR of Outer-Membrane Protein G from Escherichia Coli. ChemBioChem: A European Journal of Chemical Biology, 6(9), 1679-1684. doi:10.1002/cbic.200500132.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-DA20-1
Zusammenfassung
Uniformly 13C-,15N-labelled outer-membrane protein G (OmpG) from Escherichia coli was expressed for structural studies by solid-state magic-angle spinning (MAS) NMR. Inclusion bodies of the recombinant, labelled protein were purified under denaturing conditions and refolded in detergent. OmpG was reconstituted into lipid bilayers and several milligrams of two-dimensional crystals were obtained. Solid-state MAS NMR spectra showed signals with an apparent line width of 80-120 Hz (including homonuclear scalar couplings). Signal patterns for several amino acids, including threonines, prolines and serines were resolved and identified in 2D proton-driven spin-diffusion (PDSD) spectra.