质子化学位移各向异性的测量

doi:10.11938/cjmr20172599

摘要/Abstract

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（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.

关键词: 固体核磁共振, 综述, 化学位移各向异性(CSA), 质子, 氢键

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 (RN_n^v) 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.

Key words: solid-state NMR, review, chemical shift anisotropy (CSA), proton, hydrogen bond

中图分类号:

O482.53

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.

GE Yu-wei, LIU Mai-li, GAN Zhe-hong, LI Cong-gang. Measurements of Proton Chemical Shift Anisotropy[J]. Chinese Journal of Magnetic Resonance, 2018, 35(2): 255-267.

参考文献

[1] WYLIE B J, RIENSTRA C M. Multidimensional solid state NMR of anisotropic interactions in peptides and proteins[J]. J Chem Phys, 2008, 128(5):052207.
[2] FACELLI J C. Chemical shift tensors:Theory and application to molecular structural problems[J]. Prog Nucl Mag Res Sp, 2011, 58(3,4):176-201.
[3] SAITO H, ANDO I, RAMAMOORTHY A. Chemical shift tensor-the heart of NMR:Insights into biological aspects of proteins[J]. Prog Nucl Mag Res Sp, 2010, 57(2):181-228.
[4] BAX A, SZEVERENYI N M, MACIEL G E. Correlation of isotropic shifts and chemical-shift anisotropies by two-dimensional fourier-transform magic-angle hopping NMR-spectroscopy[J]. J Magn Reson, 1983, 52(1):147-152.
[5] LOTH K, PELUPESSY P, BODENHAUSEN G. Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy[J]. J Am Chem Soc, 2005, 127(16):6062-6068.
[6] BROUWER D H, RIPMEESTER J A. Symmetry-based recoupling of proton chemical shift anisotropies in ultrahigh-field solid-state NMR[J]. J Magn Reson, 2007, 185(1):173-178.
[7] YAO L, GRISHAEV A, CORNILESCU G, et al. The impact of hydrogen bonding on amide ¹H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy[J]. J Am Chem Soc, 2010, 132(31):10866-10875.
[8] HOU G J, PARAMASIVAM S, YAN S, et al. Multidimensional magic angle spinning NMR spectroscopy for site-resolved measurement of proton chemical shift anisotropy in biological solids[J]. J Am Chem Soc, 2013, 135(4):1358-1368.
[9] KOVER K E, BATTA G, HRUBY V J. Solution-phase chemical shift anisotropy as a promising tool to probe intermolecular interactions and peptide bond geometry:a case study on ¹⁵N-labeled Nα-t-Boc-L-valine[J]. Magn Reson Chem, 2003, 41(10):828-836.
[10] TESSARI M, MULDER F A A, BOELENS R, et al. Determination of amide proton CSA in ¹⁵N-labeled proteins using ¹H CSA/¹⁵N-¹H dipolar and ¹⁵N CSA/¹⁵N-¹H dipolar cross-correlation rates[J]. J Magn Reson, 1997, 127(1):128-133.
[11] TJANDRA N, BAX A. Solution NMR measurement of amide proton chemical shift anisotropy in ¹⁵N-enriched proteins. correlation with hydrogen bond length[J]. J Am Chem Soc, 1997, 119(34):8076-8082.
[12] CORNILESCU G, BAX A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase[J]. J Am Chem Soc, 2000, 122(41):10143-10154.
[13] BERGLUND B, VAUGHAN R W. Correlations between proton chemical shift tensors, deuterium quadrupole couplings, and bond distances for hydrogen bonds in solids[J]. J Chem Phys, 1980,73(5):2037-2043.
[14] GE Y W, HUNG I, LIU X L, et al. Measurement of amide proton chemical shift anisotropy in perdeuterated proteins using CSA amplification[J]. J Magn Reson, 2017, 284:33-38.
[15] HADDIX D C, LAUTERBUR C C. Molecular dynamics and structure of solids[J]. Natl Bur Stand, 1969:403-406.
[16] MOROZ N K, PANICH A M, GABUDA S P. Shielding anisotropy of H-bonded protons in Cs₂GeF₆·4HF[J]. J Magn Reson, 1969, 1983, 53(1):1-6.
[17] TEKELY P, PALMAS P, MUTZENHARDT P. Influence of proton chemical-shift anisotropy on magic-angle spinning spectra of hydrate crystals[J]. J Magn Reson, 1997, 127(2):238-240.
[18] IWAMIYA J H, SINTON S W, LIU H, et al. Multiple-pulse sequences for homonuclear decoupling. experimental verification[J]. J Magn Reson, 1969, 1992, 100(2):367-375.
[19] HU J Z, ALDERMAN D W, YE C H, et al. An isotropic chemical shift-chemical shift anisotropy magic-angle slow-spinning 2D NMR experiment[J]. J Magn Reson Ser A, 1993, 105(1):82-87.
[20] HOHWY M, RASMUSSEN J T, BOWER P V, et al. ¹H chemical shielding anisotropies from polycrystalline powders using MSHOT-3 based CRAMPS[J]. J Magn Reson, 1998, 133(2):374-378.
[21] PINES A, VEGA S, MEHRING M. NMR double quantum spin decoupling in solids[J]. Phys Rev, 2011, 18(1):112-125.
[22] PINES A, RUBEN D J, VEGA S, et al. New approach to high-resolution proton NMR in solids:deuterium spin decoupling by multiple-quantum transitions[J]. Phys Rev Lett, 1976, 36(36):110-113.
[23] VEGA S, SHATTUCK T W, PINES A. Fourier-transform double-quantum NMR in solids[J]. Phys Rev Lett, 1976, 37(1):43-46.
[24] ACHLAMA A M. The chemical shift and EFG tensors at the carboxylic deuterons of α-oxalic acid dihydrate[J]. J Magn Reson, 1980, 41(3):374-380.
[25] ACHLAMA A M. The chemical shift, dipolar, and quadrupolar tensors of deuterium in potassium bicarbonate[J]. J Chem Phys, 1981, 74(6):3623-3625.
[26] REX GERALD I I, BERNHARD T, HAEBERLEN U, et al. Chemical shift and electric field gradient tensors for the amide and carboxyl hydrogens in the model peptide N-acetyl-D,L-valine. Single-crystal deuterium NMR study[J]. J Am Chem Soc, 1993, 115(2):777-782.
[27] DUMA L, ABERGEL D, TEKELY P, et al. Proton chemical shift anisotropy measurements of hydrogen-bonded functional groups by fast magic-angle spinning solid-state NMR spectroscopy[J]. Chem Commun, 2008, 20:2361-2363.
[28] PANDEY M K, YARAVA J R, ZHANG R, et al. Proton-detected 3D ¹⁵N/¹H/¹H isotropic/anisotropic/isotropic chemical shift correlation solid-state NMR at 70 kHz MAS[J]. Solid State Nucl Magn Reson, 2016, 76-77:1-6.
[29] ZHANG R, MROUE K H, RAMAMOORTHY A. Proton-based ultrafast magic angle spinning solid-state NMR spectroscopy[J]. Acc Chem Res, 2017, 50(4):1105-1113.
[30] HOU G, GUPTA R, POLENOVA T, et al. A magic-angle spinning NMR method for the site-specific measurement of proton chemical-shift anisotropy in biological and organic solids[J]. Isr J Chem, 2014, 54(1,2):171-183.
[31] MOON S, CASE D A. A new model for chemical shifts of amide hydrogens in proteins[J]. J Biomol NMR, 2007, 38(2):139-150.
[32] OSAPAY K, CASE D A. A new analysis of proton chemical shifts in proteins[J]. J Am Chem Soc, 1991, 113(25):9436-9444.
[33] OSAPAY K, CASE D A. Analysis of proton chemical shifts in regular secondary structure of proteins[J]. J Biomol NMR, 1994, 4(2):215-230.
[34] SITKOFF D, CASE D A. Density functional calculations of proton chemical shifts in model peptides[J]. J Am Chem Soc, 1997, 119(50):12262-12273.
[35] DEJAEGERE A, BRYCE R A, CASE D A. An empirical analysis of proton chemical shifts in nucleic acids[J]. Acs Symposium, 1999, 732:194-206.
[36] TANG S, CASE D A. Calculation of chemical shift anisotropy in proteins[J]. J Biomol NMR, 2011, 51(3):303-312.
[37] SHARMA Y, KWON O Y, BROOKS B, et al. An ab initio study of amide proton shift tensor dependence on local protein structure[J]. J Am Chem Soc, 2002, 124(2):327-335.
[38] PARKER L L, HOUK A R, JENSEN J H. Cooperative hydrogen bonding effects are key determinants of backbone amide proton chemical shifts in proteins[J]. J Am Chem Soc, 2006, 128(30):9863-9872.
[39] SUZUKI Y, TAKAHASHI R, SHIMIZU T, et al. Intra-and intermolecular effects on ¹H chemical shifts in a silk model peptide determined by high-field solid state ¹H NMR and empirical calculations[J]. J Phys Chem B, 2009, 113(29):9756-9761.
[40] MIAH H K, BENNETT D A, IUGA D, et al. Measuring proton shift tensors with ultrafast MAS NMR[J]. J Magn Reson, 2013, 235(Supplement C):1-5.
[41] PANDEY M K, NISHIYAMA Y. Determination of NH proton chemical shift anisotropy with ¹⁴N-¹H heteronuclear decoupling using ultrafast magic angle spinning solid-state NMR[J]. J Magn Reson, 2015, 261:133-140.
[42] PANDEY M K, MALON M, RAMAMOORTHY A, et al. Composite-180° pulse-based symmetry sequences to recouple proton chemical shift anisotropy tensors under ultrafast MAS solid-state NMR spectroscopy[J]. J Magn Reson, 2015, 250(Supplement C):45-54.
[43] PANDEY M K, NISHIYAMA Y. Determination of relative orientation between ¹H CSA tensors from a 3D solid-state NMR experiment mediated through ¹H/¹H RFDR mixing under ultrafast MAS[J]. Solid State Nucl Magn Reson, 2015, 70(Supplement C):15-20.
[44] CARRAVETTA M, EDEN M, ZHAO X, et al. Symmetry principles for the design of radiofrequency pulse sequences in the nuclear magnetic resonance of rotating solids[J]. Chem Phys Lett, 2000, 321(3,4):205-215.
[45] ZHAO X, EDEN M, LEVITT M H. Recoupling of heteronuclear dipolar interactions in solid-state NMR using symmetry-based pulse sequences[J]. Chem Phys Lett, 2001, 342(3):353-361.
[46] GULLION T. Extended Chemical-Shift Modulation[J]. J Magn Reson, 1989, 85(3):614-619.
[47] RALEIGH D P, KOLBERT A C, OAS T G, et al. Enhancement of the effect of small anisotropies in magic-angle spinning nuclear magnetic resonance[J]. J Chem Soc, Faraday Trans, 1988, 84(11):3691-3711.
[48] HUNG I, GAN Z. An efficient amplification pulse sequence for measuring chemical shift anisotropy under fast magic-angle spinning[J]. J Magn Reson, 2011, 213(1):196-199.
[49] WISHART D S, SYKES B D, RICHARDS F M. The chemical shift index:a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy[J]. Biochemistry, 1992, 31(6):1647-1651.
[50] WISHART D S, SYKES B D.
[12] Chemical shifts as a tool for structure determination[J]. Methods Enzymol, 1994, 239:363-392.
[51] WISHART D, SYKES B D. The ¹³C Chemical-shift index:a simple method for the identification of protein secondary structure using ¹³C chemical-shift data[J]. J Biomol NMR, 1994, 4(2):171-180.
[52] ANDREAS L B, JAUDZEMS K, STANEK J, et al. Structure of fully protonated proteins by proton-detected magic-angle spinning NMR[J]. Proc Natl Acad Sci U S A, 2016, 113(33):9187-9192.