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Band-selective 13C Homonuclear 3D Spectroscopy for Solid Proteins at High Field with Rotor-synchronized Soft Pulses

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Abstract

We demonstrate improved 3D 13C–13C–13C chemical shift correlation experiments for solid proteins, utilizing band-selective coherence transfer, scalar decoupling and homonuclear zero-quantum polarization transfer. Judicious use of selective pulses and a z-filter period suppress artifacts with a two-step phase cycle, allowing higher digital resolution in a fixed measurement time. The novel correlation of Cali–Cali–CX (Cali for aliphatic carbons, CX for any carbon) reduces measurement time by an order of magnitude without sacrificing digital resolution. The experiment retains intensity from side-chain carbon resonances whose chemical shift dispersion is critical to minimize spectral degeneracy for large proteins with a predominance of secondary structure, such as β-sheet rich fibrillar proteins and α-helical membrane proteins. We demonstrate the experiment for the β1 immunoglobulin binding domain of protein G (GB1) and fibrils of the A30P mutant of α-synuclein, which is implicated in Parkinson’s disease. Selective pulses of duration comparable the rotor period give optimal performance, but must be synchronized with the spinning in non-trivial ways to minimize chemical shift anisotropy recoupling effects. Soft pulses with a small bandwidth-duration product are best for exciting the ~70 ppm bandwidth required for aliphatic-only dimensions.

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References

  • D. Abramovich S. Vega (1993) J. Magn. Reson. A 105 30–48 Occurrence Handle10.1006/jmra.1993.1245

    Article  Google Scholar 

  • O.N. Antzutkin R.D. Leapman J.J. Balbach R. Tycko (2002) Biochemistry 41 15436–15450 Occurrence Handle10.1021/bi0204185

    Article  Google Scholar 

  • J.J. Balbach A.T. Petkova N.A. Oyler O.N. Antzutkin D.J. Gordon S.C. Meredith R. Tycko (2002) Biophys. J. 83 1205–1216 Occurrence Handle10.1016/S0006-3495(02)75244-2

    Article  Google Scholar 

  • M. Baldus A.T. Petkova R.G. Griffin J. Herzfeld (1998) Mol. Phys. 95 1197–1207 Occurrence Handle10.1080/002689798166215

    Article  Google Scholar 

  • H. Barkhuijsen R. Beer Particlede D. Ormondt Particlevan (1987) J. Magn. Reson. 73 553–557

    Google Scholar 

  • C. Bauer R. Freeman T. Frenkiel J. Keeler A.J. Shaka (1984) J. Magn. Reson. 58 442–457

    Google Scholar 

  • A. Bax M. Ikura L.E. Kay G. Zhu (1991) J. Magn. Reson. 91 174–178

    Google Scholar 

  • A.E. Bennett R.G. Griffin (1992) J. Chem. Phys. 96 8624–8627 Occurrence Handle10.1063/1.462267 Occurrence Handle1992JChPh..96.8624B

    Article  ADS  Google Scholar 

  • A.E. Bennett C.M. Rienstra M. Auger K.V. Lakshmi R.G. Griffin (1995) J. Chem. Phys. 103 6951–6958 Occurrence Handle10.1063/1.470372 Occurrence Handle1995JChPh.103.6951B

    Article  ADS  Google Scholar 

  • N. Bloembergen (1949) Physica 15 386–426 Occurrence Handle10.1016/0031-8914(49)90114-7 Occurrence Handle1949Phy....15..386B

    Article  ADS  Google Scholar 

  • F. Castellani B.V. Rossum A. Diehl M. Schubert K. Rehbein H. Oschkinat (2002) Nature 420 98–102 Occurrence Handle10.1038/nature01070 Occurrence Handle2002Natur.420...98C

    Article  ADS  Google Scholar 

  • D.F. Clayton J.M. George (1998) Trends Neurosci. 21 249–254 Occurrence Handle10.1016/S0166-2236(97)01213-7

    Article  Google Scholar 

  • F. Delaglio S. Grzesiek G.W. Vuister G. Zhu J. Pfeifer A. Bax (1995) J. Biomol. NMR 6 277–293 Occurrence Handle10.1007/BF00197809

    Article  Google Scholar 

  • L. Duma S. Hediger L. Emsley B. Brutscher A. Bockmann (2003a) J. Am. Chem. Soc. 125 11816–11817 Occurrence Handle10.1021/ja036893n

    Article  Google Scholar 

  • L. Duma S. Hediger A. Lesage L. Emsley (2003b) J. Magn. Reson. 164 187–195 Occurrence Handle10.1016/S1090-7807(03)00187-3 Occurrence Handle2003JMagR.164..187D

    Article  ADS  Google Scholar 

  • L. Emsley G. Bodenhausen (1989) J. Magn. Reson. 82 211–221

    Google Scholar 

  • L. Emsley G. Bodenhausen (1990) Chem. Phys. Lett. 165 469–476 Occurrence Handle10.1016/0009-2614(90)87025-M Occurrence Handle1990CPL...165..469E

    Article  ADS  Google Scholar 

  • W.T. Franks D.H. Zhou B.J. Wylie B.G. Money D.T. Graesser H.L. Frericks G. Sahota C.M. Rienstra (2005) J. Am. Chem. Soc. 127 12291–12305 Occurrence Handle10.1021/ja044497e

    Article  Google Scholar 

  • H. Geen R. Freeman (1991) J. Magn. Reson. 93 93–141

    Google Scholar 

  • S. Hediger B.H. Meier N.D. Kurur G. Bodenhausen R.R. Ernst (1994) Chem. Phys. Lett. 223 283–288 Occurrence Handle10.1016/0009-2614(94)00470-6 Occurrence Handle1994CPL...223..283H

    Article  ADS  Google Scholar 

  • Heise, H., Hoyer, W., Becker, S., Andronesi, O.C., Riedel, D. and Baldus, M. (2005a) PNAS, 102, 15871–15876

  • H. Heise K. Seidel M. Etzkorn S. Becker M. Baldus (2005b) J. Magn. Reson. 173 64–74 Occurrence Handle10.1016/j.jmr.2004.11.020 Occurrence Handle2005JMagR.173...64H

    Article  ADS  Google Scholar 

  • T.C. Holdeman K.H. Gardner (2001) J. Biomol. NMR 21 383–384 Occurrence Handle10.1023/A:1013334608913

    Article  Google Scholar 

  • M. Hong (1999) J. Biomol. NMR 15 1–14 Occurrence Handle10.1023/A:1008334204412

    Article  Google Scholar 

  • J.M.S. Hutchinson R.J. Sutherland J.R. Mallard (1978) J. Phys. E: Sci. Instr. 11 217–221 Occurrence Handle10.1088/0022-3735/11/3/012 Occurrence Handle1978JPhE...11..217H

    Article  ADS  Google Scholar 

  • T.I. Igumenova A.E. McDermott (2003) J. Magn. Reson. 164 270–285 Occurrence Handle10.1016/S1090-7807(03)00239-8 Occurrence Handle2003JMagR.164..270I

    Article  ADS  Google Scholar 

  • C.P. Jaroniec J.C. Lansing B.A. Tounge M. Belenky J. Herzfeld R.G. Griffin (2001a) J. Am. Chem. Soc. 123 12929–12930 Occurrence Handle10.1021/ja016923r

    Article  Google Scholar 

  • C.P. Jaroniec B.A. Tounge J. Herzfeld R.G. Griffin (2001b) J. Am. Chem. Soc. 123 3507–3519 Occurrence Handle10.1021/ja003266e

    Article  Google Scholar 

  • L.E. Kay D. Marion A. Bax (1989) J. Magn. Reson. 84 72–84

    Google Scholar 

  • Kloepper, K.D., Woods, W.S., Winter, K.A., George, J.M. and Rienstra, C.M. (2006) Protein Express. Purif., (in press)

  • A. Kubo C.A. McDowell (1988) J. Chem. Soc. Faraday Trans. I 84 3713–3730 Occurrence Handle10.1039/f19888403713

    Article  Google Scholar 

  • E. Kupce J. Boyd I.D. Campbell (1995) J. Magn. Reson. B 106 300 Occurrence Handle10.1006/jmrb.1995.1049

    Article  Google Scholar 

  • Li, Y., Wylie, B.J. and Rienstra, C.M. (2006) J. Magn. Reson., 179, (in Press)

  • D. Marion M. Ikura R. Tschudin A. Bax (1989) J. Magn. Reson. 85 393

    Google Scholar 

  • N.C. Nielsen H. Bildsoe H.J. Jakobsen M.H. Levitt (1994) J. Chem. Phys. 101 1805–1812 Occurrence Handle10.1063/1.467759 Occurrence Handle1994JChPh.101.1805N

    Article  ADS  Google Scholar 

  • T.G. Oas R.G. Griffin M.H. Levitt (1989) J. Chem. Phys. 89 692–695 Occurrence Handle10.1063/1.455191 Occurrence Handle1988JChPh..89..692O

    Article  ADS  Google Scholar 

  • J. Pauli M. Baldus B. Rossum Particlevan H. Groot Particlede H. Oschkinat (2001) Chem. Bio. Chem. 2 272–281

    Google Scholar 

  • A.T. Petkova Y. Ishii J.J. Balbach O.N. Antzutkin R.D. Leapman F. Delaglio R. Tycko (2002) PNAS 99 16742–16747 Occurrence Handle10.1073/pnas.262663499 Occurrence Handle2002PNAS...9916742P

    Article  ADS  Google Scholar 

  • R. Powers D.S. Garrett C.J. March E.A. Frieden A.M. Gronenborn G.M. Clore (1992) Biochemistry 31 4334–4346 Occurrence Handle10.1021/bi00132a026

    Article  Google Scholar 

  • C.M. Rienstra M. Hohwy M. Hong R.G. Griffin (2000) J. Am. Chem. Soc. 122 10979–10990 Occurrence Handle10.1021/ja001092v

    Article  Google Scholar 

  • S.K. Straus T. Bremi R.R. Ernst (1996) Chem. Phys. Lett. 262 709–715 Occurrence Handle10.1016/S0009-2614(96)01143-8 Occurrence Handle1996CPL...262..709S

    Article  ADS  Google Scholar 

  • J.A. Stringer C.E. Bronnimann C.G. Mullen D.H. Zhou S.A. Stellfox Y. Li E.H. Williams C.M. Rienstra (2005) J. Magn. Reson. 173 40–48 Occurrence Handle10.1016/j.jmr.2004.11.015 Occurrence Handle2005JMagR.173...40S

    Article  ADS  Google Scholar 

  • B.Q. Sun C.M. Rienstra P.R. Costa J.R. Williamson R.G. Griffin (1997) J. Am. Chem. Soc. 119 8540–8546 Occurrence Handle10.1021/ja970073r

    Article  Google Scholar 

  • D. Suter R.R. Ernst (1982) Phys. Rev. B 25 6038–6041 Occurrence Handle10.1103/PhysRevB.25.6038 Occurrence Handle1982PhRvB..25.6038S

    Article  ADS  Google Scholar 

  • D. Suter R.R. Ernst (1985) Phys. Rev. B 32 5608–5627 Occurrence Handle10.1103/PhysRevB.32.5608 Occurrence Handle1985PhRvB..32.5608S

    Article  ADS  Google Scholar 

  • T. Szyperski D.C. Yeh D.K. Sukumaran H.N.B. Moseley G.T. Montelione (2002) PNAS 99 8009–8014 Occurrence Handle10.1073/pnas.122224599 Occurrence Handle2002PNAS...99.8009S

    Article  ADS  Google Scholar 

  • K. Takegoshi S. Nakamura T. Terao (2001) Chem. Phys. Lett. 344 631–637 Occurrence Handle10.1016/S0009-2614(01)00791-6 Occurrence Handle2001CPL...344..631T

    Article  ADS  Google Scholar 

  • M. Veshtort R.G. Griffin (2004) Chem. Phys. Chem. 5 834–850

    Google Scholar 

  • D.S. Wishart B.D. Sykes F.M. Richards (1991) J. Mol. Biol. 222 311–333 Occurrence Handle10.1016/0022-2836(91)90214-Q

    Article  Google Scholar 

  • S.G. Zech A.J. Wand A.E. McDermott (2005) J. Am. Chem. Soc. 127 8618–8626 Occurrence Handle10.1021/ja0503128

    Article  Google Scholar 

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Authors and Affiliations

  1. Department of Chemistry, Department of Biochemistry, and Center for Biophysics and Computational Biology, University of Illinois, 600 South Mathews Avenue, Urbana, IL, 61801, USA

    Donghua H. Zhou, Kathryn D. Kloepper, Kem A. Winter & Chad M. Rienstra

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  1. Donghua H. Zhou
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  2. Kathryn D. Kloepper
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  3. Kem A. Winter
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  4. Chad M. Rienstra
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Correspondence to Chad M. Rienstra.

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Zhou, D.H., Kloepper, K.D., Winter, K.A. et al. Band-selective 13C Homonuclear 3D Spectroscopy for Solid Proteins at High Field with Rotor-synchronized Soft Pulses. J Biomol NMR 34, 245–257 (2006). https://doi.org/10.1007/s10858-006-0026-6

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  • DOI: https://doi.org/10.1007/s10858-006-0026-6

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