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首页> 外文期刊>Journal of Biomolecular NMR >Empirical correlation between protein backbone N-15 and C-13 secondary chemical shifts and its application to nitrogen chemical shift re-referencing
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Empirical correlation between protein backbone N-15 and C-13 secondary chemical shifts and its application to nitrogen chemical shift re-referencing

机译：蛋白质骨架N-15和C-13二次化学位移之间的经验相关性及其在氮化学位移重新引用中的应用

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The linear analysis of chemical shifts (LACS) has provided a robust method for identifying and correcting C-13 chemical shift referencing problems in data from protein NMR spectroscopy. Unlike other approaches, LACS does not require prior knowledge of the three-dimensional structure or inference of the secondary structure of the protein. It also does not require extensive assignment of the NMR data. We report here a way of extending the LACS approach to N-15 NMR data from proteins, so as to enable the detection and correction of inconsistencies in chemical shift referencing for this nucleus. The approach is based on our finding that the secondary N-15 chemical shift of the backbone nitrogen atom of residue i is strongly correlated with the secondary chemical shift difference (experimental minus random coil) between the alpha and beta carbons of residue i - 1. Thus once alpha and beta C-13 chemical shifts are available (their difference is referencing error-free), the N-15 referencing can be validated, and an appropriate offset correction can be derived. This approach can be implemented prior to a structure determination and can be used to analyze potential referencing problems in database data not associated with three-dimensional structure. Application of the LACS algorithm to the current BMRB protein chemical shift database, revealed that nearly 35% of the BMRB entries have delta N-15 values mis-referenced by over 0.7 ppm and over 25% of them have delta H-1(N) values mis-referenced by over 0.12 ppm. One implication of the findings reported here is that a backbone N-15 chemical shift provides a better indicator of the conformation of the preceding residue than of the residue itself.
机译：化学位移的线性分析（LACS）提供了一种可靠的方法，可用于识别和校正蛋白质NMR光谱数据中的C-13化学位移参考问题。与其他方法不同，LACS不需要蛋白质的三维结构的先验知识或蛋白质二级结构的推断。它也不需要广泛分配NMR数据。我们在这里报告了一种方法，将LACS方法扩展到蛋白质的N-15 NMR数据，以便能够检测和校正该核的化学位移参考中的不一致之处。该方法基于我们的发现，即残基i的主链氮原子的N-15次级化学位移与残基i-1的α和β碳之间的次级化学位移差异（实验减去无规卷曲）密切相关。因此，一旦α和βC-13化学位移可用（它们的区别是参考无错误），就可以验证N-15参考，并可以得出适当的偏移校正。该方法可以在确定结构之前实施，并且可以用于分析与三维结构不相关的数据库数据中的潜在参考问题。 LACS算法在当前BMRB蛋白质化学位移数据库中的应用表明，将近35％的BMRB条目的N-15增量值被错误引用超过0.7 ppm，其中超过25％的H-1（N）错误引用的值超过0.12 ppm。此处报道的发现的一个暗示是，主链N-15化学位移比残基本身能更好地指示先前残基的构象。

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