Skip to main content
Log in

High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument

  • Article
  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

Abstract

Improvements are described in a shuttling field-cycling device (Redfield in Magn Reson Chem 41:753–768, 2003), designed to allow widespread access to this useful technique by configuring it as a removable module to a commercial 500 MHz NMR instrument. The main improvements described here, leading to greater versatility, high reliability and simple construction, include: shuttling provided by a linear motor driven by an integrated-control servomotor; provision of automated bucking magnets to allow fast two-stage cycling to nearly zero field; and overall control by a microprocessor. A brief review of history and publications that have used the system is followed by a discussion of topics related to such a device including discussion of some future applications. A description of new aspects of the shuttling device follows. The minimum round trip time to 1T and above is less than 0.25 s and to 0.002 T is 0.36 s. Commercial probes are used and sensitivity is that of the host spectrometer reduced only by relaxation during travel. A key element is development of a linkage that prevents vibration of the linear motor from reaching the probe.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

Notes

  1. http://www.bio.brandeis.edu/faculty/redfield.html.

References

  • Amero C, Schanda P, Ascunsion Dur A, Iyala I, Marion D, Franzetti B, Brutscher B, Boisbouvier J (2009) Fast two-dimensional NMR spectroscopy of high molecular weight assemblies. J Am Chem Soc 131:3448–3449

    Article  Google Scholar 

  • Batnagar J, Borbat P, Pollard A, Bilwes A, Freed J, Crane B (2010) Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed ESR spectroscopy. Biochemistry 49:3824–3841

    Article  Google Scholar 

  • Borbat P, Freed J (2007) Measuring distances by pulsed dipolar ESR spectroscopy: spin-labeled histidine kinases in two component signaling systems. In: Simon M, Crane B, Crane A (eds) Methods in enzymology, vol 423. Elsevier, pp 52–116

  • Brown M, Ribiero A, Williams G (1983) New view of lipid bilayer dynamics from 2H and 13C NMR relaxation time measurements. Proc Natl Acad Sci USA 80:4325–4329

    Article  ADS  Google Scholar 

  • Callabero-Manrique E, Bray J, Deutschman W, Dahlquist F, Guenza M (2007) A theory of protein dynamics to predict NMR relaxation. Biophys J 93:4128–4140

    Article  Google Scholar 

  • Chou C-Y, Chu M, Chang C-F, Huang T-h (2011) A compact high-speed mechanical sample shuttle for field-dependent high-resolution solution NMR. J Magn Reson. doi:10.1016/j.jmr.2011.12.001

  • Clarkson M, Lei M, Eisenmesser E, 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 

  • Clore M, Gronenborn A (1982) Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands attached to proteins. J Magn Reson 48:402–417

    Google Scholar 

  • Clore M, Iwahara J (2009) Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem Rev 109:4108–4139

    Article  Google Scholar 

  • Da Costa G, Mouret L, Chevanc S, Le Rumeur E, Bondon A (2007) NMR of small molecules interacting with lipids in small unilamelar vesicles. Eur Biophys J 36:933–942

    Article  Google Scholar 

  • De Angelis A, Jones D, Grant C, Park S, Mesleh M, Opella S (2005) NMR experiments on aligned samples of membrane proteins. In: James T (ed) Methods in enzymology, vol 394. Elsevier, pp 350–382

  • Diakova G, Goddard Y, Korb J-P, Bryant R (2010) Water and backbone dynamics in a hydrated protein. Biophys J 98:138–146

    Article  Google Scholar 

  • Dolainski C, Unger M, Bloom M, Bayerl T (1985) Two-dimensional exchange 2H NMR experiments of phospholipid bilayers on a spherical solid support. Phys Rev E 51:4743–4750

    Article  ADS  Google Scholar 

  • Ferrante G, Sykora S (2004) Technical aspects of fast field cycling. In: van Edik R, Bertini I (eds) Advances in inorganic chemistry, vol 57. Academic Press, pp 405–470

  • Gaede H, Gawrisch K (2003) Latteral diffusion of lipid, water, and a hydrophobic drug in multilamellar liposomes. Biophys J 85:1734–1740

    Article  Google Scholar 

  • Grosse S, Gubaydullin F, Scheelken S, Vieth H-M, Yurkovskaya A (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 

  • Gueron M (1975) Nuclear relaxation in macromolecules by paramagnetic Ions: a novel mechanism. J Magn Reson 19:58–66

    Google Scholar 

  • Hallock K, Wildman K, Lee D-K, Ramamoorthy A (2002) An innovative procedure using a sublimable solid to align bilayers for solid-state NMR studies. Biophys J 82:2499–2503

    Article  Google Scholar 

  • Hecht R, Redfield A (1963) Overhauser effect in metallic lithium and sodium. Phys Rev 132:972–977

    Article  ADS  Google Scholar 

  • Ivanov D, Redfield A (2004) Field cycling method with central transition readout for pure quadrupole resonance detection in dilute systems. J Magn Reson 166:19–27

    Article  ADS  Google Scholar 

  • Kang C, Vanoye C, Welch R, Van Horne W, Sanders C (2010) Functional delivery of a membrane protein into oocyte membranes using bicelles. Biochemistry 49:632–655

    Article  Google Scholar 

  • Kerwood D, Bolton P (1987) A sample shuttling device suitable for two-dimensional low-field NMR. J Magn Reson 75:142–146

    Google Scholar 

  • Kimmich R, Estaban A (2004) Field cycling NMR relaxometry. Prog NMR Spectrosc 44:257–320

    Article  Google Scholar 

  • Klauda J, Eldho N, Gawrisch K, Brooks B, Pastor R (2008a) Collective and noncollective modes of NMR relaxation in lipid vesicles and multilayers. J Phys Chem B112:5924–5929

    Google Scholar 

  • Klauda J, Roberts M, Redfield A, Brooks B, Pastor R (2008b) Rotation of lipids in membranes: MD simulation, 31P spin-lattice relaxation, and rigid-body dynamics. Biophys J 94:3074–3083

    Article  Google Scholar 

  • Koenig S, Brown R (1990) Field cycling relaxometry of protein solutions and tissues: implications for MRI. Prog NMR Spectrosc 22:487–567

    Article  Google Scholar 

  • Korchak S, Kiryutin A, Ivanov K, Yurkovskaya A, Grishin Y, Zimmermann H, Vieth H-M (2010) Low-field, time-resolved dynamic nuclear polarization with field cycling and high-resolution NMR detection. Appl Magn Reson 37:515–537

    Article  Google Scholar 

  • Krahn A, Lottman P, Marquardsen T, Tavernier A, Turke M-T, Reese M, Leonov A, Bennati M, Hoefer P, Engleke F, Griesinger C (2010) Shuttle DNP spectrometer with a two-center magnet. Phys Chem Chem Phys 12:5830–5840

    Article  Google Scholar 

  • Lane AN, Jenkins T, Brown T, Neidle S (1991) Interaction of beneril with the EcoRI dodecamer d(CGCGAATTCGCG)2 in solution studied by NMR. Biochemistry 30:1372–1385

    Article  Google Scholar 

  • Leftin A, Brown M (2011) An NMR database for simulations of membrane dynamics. Biochem Biophys Acta 1808:818–839

    Article  Google Scholar 

  • Legget J, Hunter R, Granwehr J, Panek R, Linde A, Horsewill J, Mcmaster J, Smith G, Kockenberger W (2010) A dedicated spectrometer for dissolution DNP NMR spectroscopy. Phys Chem Chem Phys 12:5883–5892

    Article  Google Scholar 

  • Lin J, Abaygunawardana C, Frick D, Bessman M, Mildvan A (1997) Solution structure of the quarternary Mut-T-M2+ complex and mechanism of its pyrophosphohydrolase reaction. Biochemistry 36:1199–1211

    Article  Google Scholar 

  • Lurie D, Aime S, Baroni S, Booth N, Broche L, Choi C-H, Davies G, Ismail S, ǑhǑgain D, Pine K (2010) Fast field-cycling magnetic resonance imaging. Compt Rend Physique 11:136–148

    Article  ADS  Google Scholar 

  • Palmer AG III (1997) Probing molecular motion by NMR. Curr Opin Struct Biol 7:732–737

    Article  MathSciNet  Google Scholar 

  • Pileio G, Carravata M, Levitt M (2010) Storage of nuclear magnetism as long-lived singlet order in low magnetic field. Proc Natl Acad Sci USA 107:17136–17139

    Article  ADS  Google Scholar 

  • Pu M, Fang X, Gershenson A, Redfield A, Roberts M (2009a) Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: insights into phosphatidylcholine activation and surface dilution inhibition. J Biol Chem 284:16099–16107

    Article  Google Scholar 

  • Pu M, Feng J, Redfield A, Roberts M (2009b) Enzymology with a spin-labeled phospholipase C: soluble substrate binding by 31P NMR from 0.005 to 11.7 Tesla. Biochemistry 48:8282–88284

    Article  Google Scholar 

  • Pu M, Orr A, Redfield A, Roberts M (2010) Defining specific lipid binding sites for membrane-bound phospholipase C, by 31P NMR from 0.005 to 11.7 T. J Biol Chem 285:26916–26922

    Article  Google Scholar 

  • Raschle T, Hiller S, Etzkorn M, Wagner G (2010) Nonmicellar systems for solution NMR spectroscopy of membrane proteins. Curr Opin Struct Biol 20:471–479

    Article  Google Scholar 

  • Redfield A (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 

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

    Article  Google Scholar 

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

    Article  ADS  Google Scholar 

  • Roberts M, Cui Q, Turner C, Case D, Redfield A (2004) High-resolution field-cycling NMR studies of a DNA octamers as a probe of phosphodiester dynamics and comparison with computer simulation. Biochemistry 43:3637–3650

    Article  Google Scholar 

  • Roberts M, Mohanty U, Redfield A (2009) Phospholipid reorientation at the lipid/water interface measured by high resolution field cycling 31P NMR spectroscopy. Biophys J 97:132–141

    Article  Google Scholar 

  • Shi X, Shao C, Zhang X, Zambonelli C, Redfield A, Head J, Seaton B, Roberts M (2009) Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface. J Biol Chem 284:15607–15618

    Article  Google Scholar 

  • Sivanandam V, Cai J, Redfield A, Roberts M (2009) Phosphatidylcholine “wobble” in vesicles assessed by high-resolution 13C field cycling NMR spectroscopy. J Am Chem Soc 131:3420–3421

    Article  Google Scholar 

  • Sousa D, Fernandes G, Marques G, Ribiero A, Sebastiaou P (2004) Novel pulsed switched power supply for a fast field cycling NMR spectrometer. Solid State NMR 25:160–166

    Article  Google Scholar 

  • Strombotne R, Hahn E (1964) Longitudinal nuclear spin–spin relaxation. Phys Rev A 133:1616–1629

    ADS  Google Scholar 

  • Victor K, Kavolius Y, Bryant R (2004) Magnetic relaxation dispersion probe. J Magn Reson 171:253–257

    Article  ADS  Google Scholar 

  • Victor K, Van-Quynh A, Bryant R (2005) High frequency dynamics in hemoglobin measured by magnetic relaxation dispersion. Biophys J 88:443–454

    Article  Google Scholar 

  • Wang Y, Chen W, Blair D, Pu M, Xu Y, Miller S, Redfield A, Chiles T, Roberts M (2008) Insights into the structural specificity of the cytotoxicity of 3-deoxy-phosphatidylinositols. J Am Chem Soc 130:7746–7755

    Article  Google Scholar 

  • Weitekamp DP, Zax D, Zilm K, Pines A (1983) Zero field magnetic resonance. Phys Rev Lett 50:1807–1810

    Article  ADS  Google Scholar 

Download references

Acknowledgments

This development was supported by National Institutes of Health grant GM077974, and, previously, grant CHE-0109575 from the National Science Foundation Chemical Instrumentation Program, and grant 36680-ACF from the American Chemical Society Petroleum Research Fund. Marcel Reese suggested the use of a servomotor, and its supplier, for this device. We thank our research collaborators, especially Mary Roberts, for performing much of the research reviewed here, and helping prepare the figures. David Roberts provided the photographs, and Thomas Pochapsky kindly read this manuscript. We received much technical help from many individuals in building this shuttler, especially from Frank Mello who fabricated parts for us as well as providing many useful suggestions, and Annemarie Rom-Weisenbach for expert programming. We thank Tai-huang Huang for sending us the recent paper describing the new shuttle design (Chou et al. 2011).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Alfred G. Redfield.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Redfield, A.G. 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 (2012). https://doi.org/10.1007/s10858-011-9594-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10858-011-9594-1

Keywords

Navigation