13C NMR chemical shifts can predict disulfide bond formation
13C NMR chemical shifts can predict disulfide bond formation
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DOI：
10.1023/a:1008398416292
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发表时间：
2000-10-01
影响因子：
2.7
通讯作者：
Rajarathnam, K
中科院分区：
文献类型：
--
作者：
Sharma, D;Rajarathnam, K
二硫键的存在只有用x射线晶体学才能明确地检测出来，否则必须用化学方法推断出来。在这项研究中，我们证明了C-13核磁共振化学位移是诊断二硫键的形成，并可以区分半胱氨酸在还原（自由）和氧化（二硫键）状态。利用BMRB和Sheffield数据库以及已发表的期刊，构建了半胱氨酸C-13 c - α和c - β化学位移数据库。统计分析表明，c - β位移对氧化还原态非常敏感，可以预测二硫键态。此外，在c - α / c - β化学位移图中，两种状态的化学位移作为二级结构的函数占据不同的簇。在这些结果的基础上，我们提供了预测半胱氨酸氧化还原状态的简单基本规则；这些规则可以有效地用于核磁共振结构测定，预测新的折叠，以及蛋白质折叠的研究。
The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that C-13 NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded) state. A database of cysteine C-13 C-alpha and C-beta chemical shifts was constructed from the BMRB and Sheffield databases, and published journals. Statistical analysis indicated that the C-beta shift is extremely sensitive to the redox state, and can predict the disulfide-bonded state. Further, chemical shifts in both states occupy distinct clusters as a function of secondary structure in the C-alpha/C-beta chemical shift map. On the basis of these results, we provide simple ground rules for predicting the redox state of cysteines; these rules could be used effectively in NMR structure determination, predicting new folds, and in protein folding studies.