Chinese Journal of Magnetic Resonance >

2017 , Vol. 34 >Issue 3: 257 - 265

DOI: https://doi.org/10.11938/cjmr20162528

Efficiency of Double Cross Polarization in Magic-Angle Spinning Solid-State NMR Studies on Membrane Proteins

  • SUN Yi ,
  • CHEN Yan-ke ,
  • LI Jian-ping ,
  • ZHAO Yong-xiang ,
  • YANG Jun
Expand
  • 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

Received date: 2016-05-15

  Revised date: 2017-08-01

  Online published: 2017-09-05

Fold

Abstract

The efficiency of multiple-dimensional heteronuclear correlation experiments in membrane protein studies is partially determined by the efficiency of double cross polarization (DCP). DCP is a basic block in the pulse sequences to probe the connections between the 15N and 13C nuclei. In this study, three membrane proteins were studied experimentally to determine how the dynamics properties of the proteins affect the DCP efficiency in solid-state heteronuclear correlation experiments. Under the same experimental conditions, the AQPZ protein showed the highest DCP efficiency (31%), while the EV71 2B protein had the lowest efficiency (14%) and the DAGK protein in between (23%). Longitudinal lattice relaxation time in the rotating frame (T1ρ) and dipole coupling constant (DHN) were also measured for these proteins. It was found that the DCP efficiency depended strongly on T1ρ, but only weakly on DHN. Based on the experimental data, a model to correlate the T1ρ of protein to the DCP efficiency was established, with which the DCP efficiency could be predicted by measuring the T1ρ of membrane proteins.

Key words： solid-state NMR; magic-angle spinning (MAS); membrane protein; double cross polarization (DCP); T1ρ

Cite this article

SUN Yi , CHEN Yan-ke , LI Jian-ping , ZHAO Yong-xiang , YANG Jun . Efficiency of Double Cross Polarization in Magic-Angle Spinning Solid-State NMR Studies on Membrane Proteins[J]. Chinese Journal of Magnetic Resonance, 2017 , 34(3) : 257 -265 . DOI: 10.11938/cjmr20162528

References

[1] SCHOLZ I, HUBER M, MANOLIKAS T, et al. MIRROR recoupling and its application to spin diffusion under fast magic-angle spinning[J]. Chem Phys Lett, 2008, 460(1):278-283.
[2] DE PAËPE G, LEWANDOWSKI J R, LOQUET A, et al. Proton assisted recoupling and protein structure determination[J]. J Chem Phys, 2008, 129(24):245101-245122.
[3] LEWANDOWSKI J R, DE PAËPE G, GRIFFIN R G. Proton assisted insensitive nuclei cross polarization[J]. J Am Chem Soc, 2007, 129(4):728-729.
[4] MORCOMBE C R, GAPONENKO V, BYRD R A, et al. Diluting abundant spins by isotope edited radio frequency field assisted diffusion[J]. J Am Chem Soc, 2004, 126(23):7196-7197.
[5] BALDUS M, PETKOVA A T, HERZFELD J, et al. Cross polarization in the tilted frame:assignment and spectral simplification in heteronuclear spin systems[J]. Mol Phys, 1998, 95(6):1197-1207.
[6] PINES A, GIBBY M, WAUGH J. Proton-enhanced nuclear induction spectroscopy. A method for high-resolution NMR of dilute spins in solid[J]. J Chem Phys, 1972, 56(4):1776-1777.
[7] TAKEGOSHI K, NAKAMURA S, TERAO T. 13C-1H dipolar-assisted rotational resonance in magic-angle spinning NMR[J]. Chem Phys Lett, 2001, 344(5):631-637.
[8] BJERRING M, NIELSEN N C. Solid-state NMR heteronuclear coherence transfer using phase and amplitude modulated rf irradiation at the Hartmann-Hahn sideband conditions[J]. Chem Phys Lett, 2003, 382(5):671-678.
[9] BIELECKI A, BURUM D P. Temperature dependence of 207Pb MAS spectra of solid lead nitrate. An accurate, sensitive thermometer for variable-temperature MAS[J]. J Magn Reson, Ser A, 1995, 116(2):215-220.
[10] MILDNER T, ERNST H, FREUDE D. 207Pb NMR detection of spinning-induced temperature gradients in MAS rotors[J]. Solid State Nucl Magn Reson, 1995, 5(3):269-271.
[11] HU B, AMOUREUX J P, TRÉBOSC J, et al. Through-space MP-CPMAS experiments between spin-1/2 and half-integer quadrupolar nuclei in solid-state NMR[J]. J Magn Reson, 2008, 192(1):8-16.
[12] HEDIGER S, MEIER B, ERNST R. Cross polarization under fast magic angle sample spinning using amplitude-modulated spin-lock sequences[J]. Chem Phys Lett, 1993, 213(5, 6):627-635.
[13] MCDERMOTT A. Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR[J]. Annu Rev Biophys, 2009, 38:385-403.
[14] GOOD D B, WANG S, WARD M E, et al. Conformational dynamics of a seven transmembrane helical protein anabaena sensory rhodopsin probed by solid-state NMR[J]. J Am Chem Soc, 2014, 136(7):2833-2842.
[15] PARK S H, CASAGRANDE F, DAS B B, et al. Local and global dynamics of the G protein-coupled receptor CXCR1[J]. Biochemistry, 2011, 50(12):2371-2380.
[16] JAIN S, BJERRING M, NIELSEN N C. Efficient and robust heteronuclear cross-polarization for high-speed-spinning biological solid-state NMR spectroscopy[J]. J Phys Chem Lett, 2012, 3(6):703-708.
[17] LAAGE S, MARCHETTI A, SEIN J, et al. Band-selective 1H-13C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy[J]. J Am Chem Soc, 2008, 130(51):17216-17217.
[18] KEHLET C, BJERRING M, SIVERTSEN A C, et al. Optimal control based NCO and NCA experiments for spectral assignment in biological solid-state NMR spectroscopy[J]. J Magn Reson, 2007, 188(2):216-230.
[19] HANSEN J Ø, KEHLET C, BJERRING M, et al. Optimal control based design of composite dipolar recoupling experiments by analogy to single-spin inversion pulses[J]. Chem Phys Lett, 2007, 447(1):154-161.
[20] BJERRING M, RASMUSSEN J T, KROGSHAVE R S, et al. Heteronuclear coherence transfer in solid-state nuclear magnetic resonance using a γ-encoded transferred echo experiment[J]. J Chem Phys, 2003, 119(17):8916-8926.
[21] RAYA J, HIRSCHINGER J. Application of rotor-synchronized amplitude-modulated cross-polarization in a 13C-1H spin pair under fast magic-angle spinning[J]. J Magn Reson, 1998, 133(2):341-351.
[22] YANG J, PARKANZKY P D, BODNER M L, et al. Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides[J]. J Magn Reson, 2002, 159(2):101-110.
[23] TANG X Q, ZHANG Z F, YANG J. Heating of biological samples in studies of MAS solid-state NMR[J]. Chinese J Magn Reson, 2015, 32(1):123-40. 唐新启, 张正逢, 杨俊. 生物固体核磁共振中样品发热的研究进展[J]. 波谱学杂志, 2015, 32(1):123-140.
[24] LI H. High-pressure NMR for studying protein structure and dynamics[J]. Chinese J Magn Reson, 2016, 33(1):1-26. 李华. 高压NMR在蛋白质结构和动力学研究中的应用[J]. 波谱学杂志, 2016, 33(1):1-26.
[25] SHI L C, AHMED M A M, ZHANG W R, et al. Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump-structural insights[J]. J Mol Biol, 2009, 386(4):1078-1093.
[26] FRERICKS H L, ZHOU D H, YAP L L, et al. Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex:E. coli cytochrome bo3 oxidase[J]. J Bimol NMR, 2006, 36(1):55-71.
[27] CASTELLANI F, VAN ROSSUM B, DIEHL A, et al. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy[J]. Nature, 2002, 420(6911):98-102.
[28] KOLODZIEJSKI W, KLINOWSKI J. Kinetics of cross-polarization in solid-state NMR:a guide for chemists[J]. Chem Rev, 2002, 102(3):613-628.
[29] BORGNIA M J, KOZONO D, CALAMITA G, et al. Functional reconstitution and characterization of AqpZ, the E. coli water channel protein[J]. J Mol Biol, 1999, 291(5):1169-1179.
[30] CHEN Y K, ZHANG Z F, TANG X Q, et al. Conformation and topology of diacylglycerol kinase in E. coli membranes revealed by solid-state NMR spectroscopy[J]. Angew Chem Int Ed, 2014, 53(22):5624-5628.
[31] VAN HORN W D, SANDERS C R. Prokaryotic diacylglycerol kinase and undecaprenol kinase[J]. Annu Rev Biophys, 2012, 41:81-82.
[32] VAN HORN W D, KIM H J, ELLIS C D, et al. Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase[J]. Science, 2009, 324(5935):1726-1729.
[33] NIU Z, ZHAO W J, ZHANG Z F, et al. The molecular structure of alzheimer β-amyloid fibrils formed in the presence of phospholipid vesicles[J]. Angew Chem Int Ed, 2014, 53(35):9294-9297.
[34] ZHANG Z F, CHEN Y K, TANG X Q, et al. Solid-state NMR shows that dynamically different domains of membrane proteins have different hydration dependence[J]. J Phys Chem B, 2014, 118(32):9553-9564.
[35] XIE S Q, WANG K, YU W J, et al. DIDS blocks a chloride-dependent current that is mediated by the 2B protein of enterovirus 71[J]. Cell Res, 2011, 21(8):1271-1275.
[36] RALEIGH D, LEVITT M, GRIFFIN R. Rotational resonance in solid state NMR[J]. Chem Phys Lett, 1988, 146(1):71-6.
[37] MORCOMBE C R, ZILM K W. Chemical shift referencing in MAS solid state NMR[J]. J Magn Reson, 2003, 162(2):479-486.
[38] D'ESPINOSE DE LACAILLERIE J B, BARBERON F, ROMANENKO K V, et al. 95Mo magic angle spinning NMR at high field:improved measurements and structural analysis of the quadrupole interaction in monomolybdates and isopolymolybdates[J]. J Phys Chem B, 2005, 109(29):14033-14042.
[39] METZ G, WU X L, SMITH S O. Ramped-amplitude cross polarization in magic-angle-spinning NMR[J]. J Magn Reson, Ser A, 1994, 110(2):219-227.
[40] HEDIGER S, MEIER B, ERNST R. Adiabatic passage Hartmann-Hahn cross polarization in NMR under magic angle sample spinning[J]. Chem Phys Lett, 1995, 240(5):449-456.
[41] LOENING N M, BJERRING M, NIELSEN N C, et al. A comparison of NCO and NCA transfer methods for biological solid-state NMR spectroscopy[J]. J Magn Reson, 2012, 214:81-90.
[42] CADY S D, HONG M. Effects of amantadine on the dynamics of membrane-bound influenza A M2 transmembrane peptide studied by NMR relaxation[J]. J Bimol NMR, 2009, 45(1,2):185-196.
[43] HUSTER D, XIAO L S, HONG M. Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain[J]. Biochemistry, 2001, 40(25):7662-7674.
[44] LINSER R, BARDIAUX B, ANDREAS L B, et al. Solid-state NMR structure determination from diagonal-compensated, sparsely nonuniform-sampled 4D proton-proton restraints[J]. J Am Chem Soc, 2014, 136(31):11002-110010.
[45] QUINN C M, MCDERMOTT A E. Monitoring conformational dynamics with solid-state R 1ρ experiments[J]. J Bimol NMR, 2009, 45(1,2):5-8.
[46] QUINN C M, MCDERMOTT A E. Quantifying conformational dynamics using solid-state R 1ρ experiments[J]. J Magn Reson, 2012, 222:1-7.
[47] FRANKS W T, KLOEPPER K D, WYLIE B J, et al. Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins[J]. J Bimol NMR, 2007, 39(2):107-131.
[48] FRANKS W T, ZHOU D H, WYLIE B J, et al. Magic-angle spinning solid-state NMR spectroscopy of the β1 immunoglobulin binding domain of protein G (GB1):15N and 13C chemical shift assignments and conformational analysis[J]. J Am Chem Soc, 2005, 127(35):12291-12305.
[49] FRANKS W T. Biomolecular solid-state nuclear magnetic resonance methods for spectral assignment and high-resolution structure determination of proteins[M]. Urbana:Butterworths, 2007.
[50] ZHAO X, EDÉN 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.
[51] FU R Q, HU J, CROSS T A. Towards quantitative measurements in solid-state CPMAS NMR:A Lee-Goldburg frequency modulated cross-polarization scheme[J]. J Magn Reson, 2004, 168(1):8-17.
Options
Outlines

/

〈 〉

Copyright © 2017 Editorial Board of Chinese Journal of Magnetic Resonance
Powered by Beijing Magtech Co. Ltd