Solid‐State Magic‐Angle Spinning NMR of Outer‐Membrane Protein G from  Escherichia coli | Zendy

Hiller Matthias | Zendy; Krabben Ludwig | Zendy; Vinothkumar Kutti R. | Zendy; Castellani Federica | Zendy; van Rossum BarthJan | Zendy; Kühlbrandt Werner | Zendy; Oschkinat Hartmut | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

Solid‐State Magic‐Angle Spinning NMR of Outer‐Membrane Protein G from Escherichia coli

Author(s) -

Hiller Matthias,

Krabben Ludwig,

Vinothkumar Kutti R.,

Castellani Federica,

van Rossum BarthJan,

Kühlbrandt Werner,

Oschkinat Hartmut

Publication year - 2005

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200500132

Subject(s) - magic angle spinning , escherichia coli , solid state nuclear magnetic resonance , spinning , bacterial outer membrane , chemistry , membrane , magic angle , materials science , crystallography , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , stereochemistry , physics , biochemistry , polymer chemistry , gene

Uniformly 13 C‐, 15 N‐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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research