Resonance Assignments of Lowly Populated and Unstable Enzyme Intermediate Complex under Real-Time Conditions.
Resonance Assignments of Lowly Populated and Unstable Enzyme Intermediate Complex under Real-Time Conditions.
复制标题
实时条件下低密度且不稳定的酶中间体复合物的共振分配。
DOI：
10.1002/cbic.201900240
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发表时间：
2019
期刊：
影响因子：
3.2
通讯作者：
Su Xun Cheng
中科院分区：
文献类型：
--
作者：
Chen Jia Liang;Wang Xiao;Xiao Yu Hao;Su Xun Cheng
Unstable and low‐abundance protein complexes represent a large family of transient protein complexes that are difficult to characterize, even by means of high‐resolution NMR spectroscopy. A method to assign the NMR signals of these unstable complexes through a combination of selective isotope labeling of amino acids in a protein and site‐specific labeling the protein with a paramagnetic tag is presented herein. By using this method, the resonances of unstable thioester intermediate complex (lifetime <5 h and highest concentration ≈20 μm) generated byStaphylococcus aureussortase A and its peptide substrate under a real‐time reaction have been assigned.
