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

Lena S. Sal | Zendy; Finn L. Aachmann | Zendy; HwaYoung Kim | Zendy; Vadim N. Gladyshev | Zendy; Alexander Dikiy | Zendy

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

Author(s) -

Lena S. Sal,

Finn L. Aachmann,

HwaYoung Kim,

Vadim N. Gladyshev,

Alexander Dikiy

Publication year - 2007

Publication title -

biomolecular nmr assignments

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.359

H-Index - 16

eISSN - 1874-2718

pISSN - 1874-270X

DOI - 10.1007/s12104-007-9039-7

Subject(s) - methionine , selenocysteine , cysteine , sulfoxide , recombinant dna , methionine sulfoxide , chemistry , biochemistry , methionine sulfoxide reductase , carbon 13 nmr , stereochemistry , amino acid , enzyme , organic chemistry , gene

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, 13C and 15N NMR assignment of the reduced form of this mammalian protein.

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