High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe

Abstract

Field-dependent NMR studies of bio-molecular systems using a sample shuttling hardware operating on a high-field NMR apparatus have provided valuable structural and dynamic information. We have recently published a design of a compact sample transportation device, called “field-cycler”, which was installed in a commercial spectrometer and which provided highly precise positioning and stability during high speed shuttling. In this communication, we demonstrate the first use of a sample shuttling device on a commercial high field standard bore NMR spectrometer, equipped with a commercial triple resonance cryogenically cooled NMR probe. The performance and robustness of the hardware operating in 1D and 2D field cycling experiments, as well as the impact of the sample shuttling time on the signal intensity are discussed.

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References

  1. Akasaka K, Ishima R, Shibata S (1990) Proton spin relaxation in biopolymers at high magnetic fields. Phys B Condens Matter 164:163–179

    ADS  Article  Google Scholar 

  2. Akke M, Skelton NJ, Kordel J, Palmer AG, Chazin WJ (1993) Effects of ion binding on the backbone dynamics of calbindin D9 k determined by nitrogen-15 NMR relaxation. Biochemistry 32:9832–9844

    Article  Google Scholar 

  3. Arthur G, Palmer WJF III, Cavanagh John, Sketon Nicholas J, Rance Mark (2006) Protein NMR spectroscopy: principles and practice, 2nd edn. Academic Press Inc, Cambridge

    Google Scholar 

  4. Black RD, Early TA, Roemer PB, Mueller OM, Mogrocampero A, Turner LG, Johnson GA (1993) A high-temperature superconducting receiver for nuclear-magnetic-resonance microscopy. Science 259:793–795

    ADS  Article  Google Scholar 

  5. Charlier C et al (2013) Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry. J Am Chem Soc 135:18665–18672

    Article  Google Scholar 

  6. Chou CY, Chu M, Chang CF, Huang TH (2012) A compact high-speed mechanical sample shuttle for field-dependent high-resolution solution NMR. J Magn Reson 214:302–308

    ADS  Article  Google Scholar 

  7. Chou C-Y, Ferrage F, Aubert G, Sakellariou D (2015) Simple method for the generation of multiple homogeneous field volumes inside the bore of superconducting magnets. Sci Rep 5:12200

    ADS  Article  Google Scholar 

  8. Clarkson MW, Lei M, Eisenmesser EZ, Labeikovsky W, Redfield A, Kern D (2009) Mesodynamics in the SARS nucleocapsid measured by NMR field cycling. J Biomol NMR 45:217–225

    Article  Google Scholar 

  9. Farrow NA et al (1994) Backbone dynamics of a free and a phosphopeptide-complexed Src homology 2 domain studied by 15 N NMR relaxation. Biochemistry 33:5984–6003

    Article  Google Scholar 

  10. Grosse S, Gubaydullin F, Scheelken H, Vieth HM, Yurkovskaya AV (1999) Field cycling by fast NMR probe transfer: design and application in field-dependent CIDNP experiments. Appl Magn Reson 17:211–225

    Article  Google Scholar 

  11. Kimmich R, Anoardo E (2004) Field-cycling NMR relaxometry. Prog Nucl Magn Reson Spectrosc 44:257–320

    Article  Google Scholar 

  12. Kovacs H, Moskau D, Spraul M (2005) Cryogenically cooled probes—a leap in NMR technology. Prog Nucl Magn Reson Spectrosc 46:131–155

    Article  Google Scholar 

  13. Krahn A et al (2010) Shuttle DNP spectrometer with a two-center magnet. Phys Chem Chem Phys 12:5830–5840

    Article  Google Scholar 

  14. Noack F (1986) NMR field-cycling spectroscopy—Principles and applications. Prog Nucl Magn Reson Spectrosc 18:171–276

    Article  Google Scholar 

  15. Nusser W, Kimmich R (1990) Protein backbone fluctuations and NMR field-cycling relaxation spectroscopy. J Phys Chem-Us 94:5637–5639

    Article  Google Scholar 

  16. Redfield AG (2003) Shuttling device for high-resolution measurements of relaxation and related phenomena in solution at low field, using a shared commercial 500 MHz NMR instrument. Magn Reson Chem 41:753–768

    Article  Google Scholar 

  17. Redfield A (2012) High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument. J Biomol NMR 52:159–177

    Article  Google Scholar 

  18. Reese M et al (2008) Construction of a liquid-state NMR DNP shuttle spectrometer: first experimental results and evaluation of optimal performance characteristics. Appl Magn Reson 34:301–311

    Article  Google Scholar 

  19. Roberts MF, Redfield AG (2004a) High-resolution P-31 field cycling NMR as a probe of phospholipid dynamics. J Am Chem Soc 126:13765–13777

    Article  Google Scholar 

  20. Roberts MF, Redfield AG (2004b) Phospholipid bilayer surface configuration probed quantitatively by P-31 field-cycling NMR. Proc Natl Acad Sci USA 101:17066–17071

    ADS  Article  Google Scholar 

  21. Roberts MF, Cui Q, Turner CJ, Case DA, Redfield AG (2004) High-resolution field-cycling NMR studies of a DNA octamer as a probe of phosphodiester dynamics and comparison with computer simulation. Biochemistry 43:3637–3650

    Article  Google Scholar 

  22. Styles P, Soffe NF, Scott CA, Crag DA, Row F, White DJ, and White PCJ (1984) A high-resolution NMR probe in which the coil and preamplifier are cooled with liquid helium. J Magn Reson 60:397–404

    ADS  Google Scholar 

  23. Swanson SD, Kennedy SD (1993) A sample-shuttle nuclear-magnetic-relaxation-dispersion spectrometer. J Magn Reson Ser A 102:375–377

    ADS  Article  Google Scholar 

  24. Thakur CS, Luo Y, Chen B, Eldho NV, Dayie TK (2012) Biomass production of site selective 13C/15 N nucleotides using wild type and a transketolase E. coli mutant for labeling RNA for high resolution NMR. J Biomol NMR 52:103–114

    Article  Google Scholar 

  25. Wagner S, Dinesen TR, Rayner T, Bryant RG (1999) High-resolution magnetic relaxation dispersion measurements of solute spin probes using a dual-magnet system. J Magn Reson 140:172–178

    ADS  Article  Google Scholar 

  26. Yanagisawa Y et al (2008) Towards beyond-1 GHz solution NMR: internal 2H lock operation in an external current mode. J Magn Reson 192:329–337

    ADS  Article  Google Scholar 

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Acknowledgments

We greatly acknowledge Dr. Sophie Zinn-Justin (CEA) for stimulating discussions and for allowing us access to the 700 MHz spectrometer, Dr. Nikolas Birlirakis (ENS) for useful comments on the manuscript and Dr. F. Ferrage (ENS) for comments and suggestions. We would like to give the special acknowledgement to Dr. Jan Marchant and the labs of Prof. Michael F. Summers and Prof. Kwaku T. Dayie in Maryland University, USA, for the UUCG tetra-loop RNA sample preparation. We also thank Mr. Angelo Guiga and the staffs in the Academia Sinica Machine Shop, Taiwan, especially Mr. Cherng-Yin Lin, for the production of the high-precision hardware. This work is supported by ERC grants 2F4BIODYN and R-EVOLUTION-M-R (StG 205119), ANR DYN-IDP in France, and NSC 102-2113-M-001-010 from The National Science Council, The Republic of China.

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Correspondence to Tai-huang Huang.

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Chou, C., Chu, M., Chang, C. et al. High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe. J Biomol NMR 66, 187–194 (2016). https://doi.org/10.1007/s10858-016-0066-5

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Keywords

  • Field cycling
  • Protein dynamics
  • High-resolution
  • Relaxometry
  • Sensitivity
  • Cryo-probes