Article

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

  • Lena S. SalAffiliated withDepartment of Biotechnology, Norwegian University of Science and Technology
  • , Finn L. AachmannAffiliated withDepartment of Biotechnology, Norwegian University of Science and Technology
  • , Hwa-Young KimAffiliated withDepartment of Biochemistry and Molecular Biology, Yeungnam University College of Medicine
  • , Vadim N. GladyshevAffiliated withDepartment of Biochemistry, University of Nebraska
  • , Alexander DikiyAffiliated withDepartment of Biotechnology, Norwegian University of Science and Technology Email author 

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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 reductase MsrB Selenium Selenocysteine