Peptide backbone conformation by solid-state nuclear magnetic resonance spectroscopy
Peptide backbone conformation by solid-state nuclear magnetic resonance spectroscopy
复制标题
通过固态核磁共振波谱分析肽骨架构象
DOI：
10.1039/f19888403803
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
S. Opella
中科院分区：
文献类型：
--
作者：
P. Stewart;R. Tycko;S. Opella
固态14 N NMR光谱用于确定单晶中肽N-乙酰基-L-缬氨酰-L-亮氨酸和L-丙氨酰甘氨酰-甘氨酸的骨架结构。这些样品提供了肽键中甘氨酰和非甘氨酰残基的实例。通过固态NMR光谱和X射线衍射确定的结构之间有很好的一致性，表明固态NMR光谱可以在不使用同位素标记的情况下描述肽骨架结构。
Solid-state 14N NMR spectroscopy is used to determine the backbone structure of the peptides N-acetyl-L-valyl-L-leucine and L-alanylglycyl-glycine in single crystals. These samples provide examples of both glycyl and non-glycyl residues in peptide linkages. There is good agreement between the structures determined by solid-state NMR spectroscopy and X-ray diffraction, demonstrating that solid-state NMR spectroscopy can describe peptide backbone structures without the use of isotopic labels.