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质子化学位移各向异性的测量

  • 葛玉玮 ,
  • 刘买利 ,
  • 甘哲宏 ,
  • 李从刚
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  • 1. 波谱与原子分子物理国家重点实验室, 武汉磁共振中心(中国科学院 武汉物理与数学研究所), 湖北 武汉 430071;
    2. 中国科学院大学, 北京 100049;
    3. Center of Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310, USA

收稿日期: 2017-10-25

  网络出版日期: 2017-11-30

基金资助

国家自然科学基金资助项目(21575156);国家重点基础研究发展计划(“973”计划)资助项目(2017YFA0505400).

Measurements of Proton Chemical Shift Anisotropy

  • GE Yu-wei ,
  • LIU Mai-li ,
  • GAN Zhe-hong ,
  • LI Cong-gang
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  • 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan(Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences), Wuhan 430071, China;
    2. University of Chinese Academy of Sciences, Beijing 100049, China;
    3. Center of Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310, USA

Received date: 2017-10-25

  Online published: 2017-11-30

摘要

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(RNnv)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.

本文引用格式

葛玉玮 , 刘买利 , 甘哲宏 , 李从刚 . 质子化学位移各向异性的测量[J]. 波谱学杂志, 2018 , 35(2) : 255 -267 . DOI: 10.11938/cjmr20172599

Abstract

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.

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