Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins
Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins
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DOI：
10.1021/ja0582206
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发表时间：
2006-03-29
影响因子：
15
通讯作者：
Pierattelli, R
中科院分区：
文献类型：
--
作者：
Bermel, W;Bertini, I;Pierattelli, R
天然未折叠蛋白发挥着重要的生理作用。这些蛋白质不会结晶，所以核磁共振是唯一能够提供结构和动态信息的技术。然而，在未折叠的蛋白质中，质子的化学位移分散性很差，导致了共振分配的严重问题。我们基于两个无质子实验设计了一个新的策略，一个CBCACON−IPAP和一个新的COCON−IPAP，它允许直接和明确的主干异核分配天然展开的蛋白质α-突触核蛋白。
Natively unfolded proteins are increasingly recognized to play important physiological roles. These proteins do not crystallize, so NMR is the only technique able to provide structural and dynamic information. However, in unfolded proteins, the proton chemical shift dispersion is poor, causing severe problems in resonance assignment. We designed a novel strategy based on twoprotonlessexperiments, a CBCACON−IPAP and a novel COCON−IPAP, that permits a straightforward and unequivocal backbone heteronuclear assignment of the natively unfolded protein α-synuclein.