Biomolecular NMR Assignments

, Volume 1, Issue 1, pp 131–133

NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus

Authors

  • Lena S. Sal
    • Department of BiotechnologyNorwegian University of Science and Technology
  • Finn L. Aachmann
    • Department of BiotechnologyNorwegian University of Science and Technology
  • Hwa-Young Kim
    • Department of Biochemistry and Molecular BiologyYeungnam University College of Medicine
  • Vadim N. Gladyshev
    • Department of BiochemistryUniversity of Nebraska
    • Department of BiotechnologyNorwegian University of Science and Technology
Article

DOI: 10.1007/s12104-007-9039-7

Cite this article as:
Sal, L.S., Aachmann, F.L., Kim, H. et al. Biomol NMR Assign (2007) 1: 131. doi:10.1007/s12104-007-9039-7

Abstract

Isotopically labeled, 15N and 15N/13C forms of recombinant methionine-r-sulfoxide reductase 1 (MsrB1, SelR) from Mus musculus were produced, in which catalytic selenocysteine was replaced with cysteine. We report here the 1H, 15N and 13C NMR assignment of the reduced form of this mammalian protein.

Keywords

Methionine sulfoxide reductaseMsrBSeleniumSelenocysteine

Copyright information

© Springer Science+Business Media B.V. 2007