English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse
  1. View item / 
  2. Item Summary

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

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

MPS-Authors
/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;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DA20-1
Abstract
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.