质子化学位移各向异性的测量

测量质子化学位移各向异性（CSA）有助于表征分子结构与其动力学,但由于¹H-¹H同核偶极耦合相互作用很强及质子各向异性化学位移较小,测量质子化学位移各向异性仍具有巨大挑战,特别是对含有多种质子的生物大分子,如蛋白质.本文简要综述了测量质子化学位移各向异性的方法,包括同核去耦慢速魔角旋转方法、超快魔角旋转方法、对称重耦（RN_n^v）方法、xCSA方法以及量子化学计算方法.我们重点介绍了在高速魔角旋转条件下蛋白质氨基质子化学位移各向异性的测量及它们与氢键长度、蛋白质二级结构之间的关系.

Measurements of Proton Chemical Shift Anisotropy

1H chemical shift anisotropy (CSA) measurements are useful for understanding molecule structure and dynamics. However, technically it remains a challenge due to strong 1H-1H homonuclear dipolar coupling interaction and relatively small 1H chemical shift anisotropy, especially in proteins with multiple proton sites. Here the current methods for 1H chemical shift anisotropy measurement are reviewed, including homonuclear decoupling slow magic angle spinning, ultrafast magic angle spinning, symmetry-based recoupling (RNnv) method, xCSA and quantum chemical calculations. Measurements of protein amide proton chemical shift anisotropy using solid state nuclear magnetic resonance (NMR) under fast magic angle spinning and correlations of amide proton chemical shift anisotropy with protein secondary structure/hydrogen bond length are discussed.