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小家鼠甲硫氨酸亚砜还原酶B1的1H、13C和15N谱的核磁共振归属

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

作者信息

Sal Lena S, Aachmann Finn L, Kim Hwa-Young, Gladyshev Vadim N, Dikiy Alexander

机构信息

Department of Biotechnology, Norwegian University of Science and Technology, Sem Saelands vei 6/8, Trondheim 7491, Norway.

出版信息

Biomol NMR Assign. 2007 Jul;1(1):131-3. doi: 10.1007/s12104-007-9039-7. Epub 2007 Jul 31.

DOI:10.1007/s12104-007-9039-7
PMID:19636847
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, 13C and 15N NMR assignment of the reduced form of this mammalian protein.

摘要

我们制备了来自小家鼠的重组蛋氨酸 - r - 亚砜还原酶1(MsrB1,SelR)的同位素标记形式,即15N和15N/13C形式,其中催化性硒代半胱氨酸被半胱氨酸取代。我们在此报告这种哺乳动物蛋白还原形式的1H、13C和15N NMR归属。

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Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis.
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J Biol Chem. 2010 Oct 22;285(43):33315-33323. doi: 10.1074/jbc.M110.132308. Epub 2010 Jul 5.