AN EFFICIENT NMR APPROACH FOR OBTAINING SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS OF LARGER PROTEINS BASED ON MULTIPLE ISOTOPIC LABELING
AN EFFICIENT NMR APPROACH FOR OBTAINING SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS OF LARGER PROTEINS BASED ON MULTIPLE ISOTOPIC LABELING
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DOI：
10.1016/0014-5793(90)81528-v
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发表时间：
1990-06-18
期刊：
影响因子：
3.5
通讯作者：
BAX, A
中科院分区：
文献类型：
--
作者：
IKURA, M;KRINKS, M;BAX, A
通过同时将不同程度的13C和15N标记的氨基酸结合到蛋白质中，观察到与13C1标记残基直接相邻的15N核的特征不对称二联体样图案，为蛋白质的大量独特的二肽片段提供了明确的识别。通过记录多个键相关谱，可以从这种选择性标记的蛋白质中获得额外的指认和定性的结构信息。演示了与钙络合的蛋白质钙调蛋白的过程。
By simultaneously incorporating in a protein13C-carbonyl- and15N-labeled amino acids with different levels of enrichment, characteristic asymmetric doublet-like patterns are observed for15N nuclei that are directly adjacent to the13C1-labeled residues, providing unambiguous identification of a large number of unique dipeptide fragments of the protein. Additional assignments and qualitative structural information can be obtained from such a selectively labeled protein by recording multiple bond correlation spectra. The procedure is demonstrated for the protein calmodulin, complexed with calcium.