Letter to the editor: 1H, 15N, and 13C NMR backbone assignments and secondary structure of the C-terminal recombinant fragment of auxilin including the J-domain.
Letter to the editor: 1H, 15N, and 13C NMR backbone assignments and secondary structure of the C-terminal recombinant fragment of auxilin including the J-domain.
复制标题
致编辑的信：辅助素 C 端重组片段（包括 J 结构域）的 1H、15N 和 13C NMR 主链分配和二级结构。
DOI：
10.1023/a:1008353226591
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发表时间：
2000
影响因子：
2.7
通讯作者：
Eisenberg,E
中科院分区：
文献类型：
--
作者：
Han,CJ;Gruschus,JM;Greener,T;Greene,LE;Ferretti,J;Eisenberg,E
Methods and resultsBovine auxilin was truncated to give the 20 kDa C-terminal recombinant protein Aux20. Aux20 was expressed as a glutathione S-transferase (GST) fusion protein. The 15N and 15N/13C labeled fusion proteins were purified by glutathione affinity chromatography. The Aux20 was cleaved from the fusion protein using PreScission protease (Amersham Pharmacia) and then concentrated. The final NMR sample contained Aux20 at a concentration of ca. 1.5 mM in 5 mM 16D-EDTA, 25 mM phosphate buffer (pH 7.0) of 90% H2O/10% D2O.
