Robustelli Paul, Cavalli Andrea, Vendruscolo Michele
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Structure. 2008 Dec 10;16(12):1764-9. doi: 10.1016/j.str.2008.10.016.
Solid-state NMR spectroscopy does not require proteins to form crystalline or soluble samples and can thus be applied under a variety of conditions, including precipitates, gels, and microcrystals. It has recently been shown that NMR chemical shifts can be used to determine the structures of the native states of proteins in solution. By considering the cases of two proteins, GB1 and SH3, we provide an initial demonstration here that this type of approach can be extended to the use of solid-state NMR chemical shifts to obtain protein structures in the solid state without the need for measuring interatomic distances.
固态核磁共振光谱法不要求蛋白质形成晶体或可溶样品，因此可以在多种条件下应用，包括沉淀物、凝胶和微晶。最近有研究表明，核磁共振化学位移可用于确定溶液中蛋白质天然状态的结构。通过考虑两种蛋白质GB1和SH3的情况，我们在此初步证明，这种方法可以扩展到利用固态核磁共振化学位移来获得固态蛋白质结构，而无需测量原子间距离。
