Biomolecular NMR Assignments

, Volume 8, Issue 2, pp 409–413

1H, 13C and 15N resonance assignments for the full-length mammalian cytochrome b5 in a membrane environment

Authors

  • Subramanian Vivekanandan
    • Department of Chemistry and BiophysicsUniversity of Michigan
  • Shivani Ahuja
    • Department of Chemistry and BiophysicsUniversity of Michigan
  • Sang-Choul Im
    • Department of AnesthesiologyUniversity of Michigan
    • VA Medical Center
  • Lucy Waskell
    • Department of AnesthesiologyUniversity of Michigan
    • VA Medical Center
    • Department of Chemistry and BiophysicsUniversity of Michigan
Article

DOI: 10.1007/s12104-013-9528-9

Cite this article as:
Vivekanandan, S., Ahuja, S., Im, S. et al. Biomol NMR Assign (2014) 8: 409. doi:10.1007/s12104-013-9528-9

Abstract

Microsomal cytochrome b5 plays a key role in the oxidation of a variety of exogenous and endogenous compounds, including drugs, fatty acids, cholesterol and steroid hormones. To better understand its functional properties in a membrane mimic environment, we carried out high-resolution solution NMR studies. Here we report resonance assignments for full-length rabbit cytochrome b5 embedded in dodecylphosphocholine micelles.

Keywords

Cytochrome b5Membrane proteinHeteronuclear NMR

Copyright information

© Springer Science+Business Media Dordrecht 2013