Marassi Francesca M, Opella Stanley J
J Biomol NMR. 2002 Jul;23(3):239-42. doi: 10.1023/a:1019887612018.
The structures of proteins are mapped onto the patterns of resonances in NMR spectra of aligned samples. This is most clearly illustrated with Pisa wheels of helical membrane proteins, where the distinctive 'wheel-like' patterns of resonances reflect the tilt and rotation of the helices in the bilayers. These patterns contain both structural and assignment information. This Communication describes a simple way of using this information to resolve angular ambiguities inherent in orientational constraints derived from NMR data. This contributes to the use of solid-state NMR of aligned samples for protein structure determination.
蛋白质的结构被映射到定向样品核磁共振谱中的共振模式上。这在螺旋膜蛋白的比萨轮图中体现得最为明显，其中独特的“轮状”共振模式反映了双层膜中螺旋的倾斜和旋转。这些模式包含结构和归属信息。本通讯描述了一种利用此信息解决核磁共振数据导出的取向约束中固有的角度模糊性的简单方法。这有助于将定向样品的固态核磁共振用于蛋白质结构测定。
