Encyclopedia of Biophysics

Living Edition
| Editors: Gordon Roberts, Anthony Watts, European Biophysical Societies

Relaxation Dispersion

  • John D. Persons
  • Shahid N. Khan
  • Rieko Ishima
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-35943-9_342-1

Synonyms

Introduction

In the NMR field, the term “relaxation dispersion” refers to the dependence of the spin relaxation rate on the magnetic field strength. Typically either the static field, B0, provided by the spectrometer or the radio-frequency (RF) field, B1, generated by the probe transmitter coil is varied over a wide range. The dependence of spin relaxation on B0 has been used to characterize relaxation mechanisms and spectral density functions (Koenig and Schillinger 1969; Kimmich 1979; Noack 1986). Its biophysics application includes paramagnetic interaction with proteins and residence times of water molecules in proteins to be obtained (Bertini et al. 1993; Halle and Denisov 1995). This B0-dependent relaxation dispersion experiment is also called “nuclear magnetic relaxation dispersion (NMRD),” “relaxometry,” or “field cycling,” in which the longitudinal relaxation rate, R1, is measured as a...

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References

  1. Akke M, Palmer AG (1996) Monitoring macromolecular motions on microsecond to millisecond time scales by R1ρ−R1 constant relaxation time NMR spectroscopy. J Am Chem Soc 118:911–912CrossRefGoogle Scholar
  2. Bertini I, Briganti F, Xia ZC, Luchinat C (1993) Nuclear magnetic relaxation dispersion studies of Hexaaquo Mn(II) ions in water-glycerol mixtures. J Magn Reson A 101:198–201CrossRefGoogle Scholar
  3. Davis DG, Perlman ME, London RE (1994) Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T-1-rho and T-2 (Cpmg) methods. J Magn Reson Ser B 104:266–275CrossRefGoogle Scholar
  4. Halle B, Denisov VP (1995) A new view of water dynamics in immobilized proteins. Biophys J 69:242–249CrossRefPubMedPubMedCentralGoogle Scholar
  5. Hansen DF, Vallurupalli P, Kay LE (2008) An improved (15)N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins. J Phys Chem B 112:5898–5904CrossRefPubMedGoogle Scholar
  6. Ishima R (2014) CPMG relaxation dispersion. Methods Mol Biol 1084:29–49CrossRefPubMedGoogle Scholar
  7. Jiang B, Yu B, Zhang X, Liu M, Yang D (2015) A (15)N CPMG relaxation dispersion experiment more resistant to resonance offset and pulse imperfection. J Magn Reson 257:1–7CrossRefPubMedGoogle Scholar
  8. Kimmich R (1979) Field cycling in NMR relaxation spectroscopy: applications in biological, chemical and polymer physics. Bull Magn Reson 1:195–218Google Scholar
  9. Koenig SH, Schillinger WE (1969) Nuclear magnetic relaxation dispersion in protein solutions. J Biol Chem 244:3283–3289PubMedGoogle Scholar
  10. Korzhnev DM, Kay LE (2008) Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Acc Chem Res 41:442–451CrossRefPubMedGoogle Scholar
  11. Loria JP, Berlow RB, Watt ED (2008) Characterization of enzyme motions by solution NMR relaxation dispersion. Acc Chem Res 41:212–221CrossRefGoogle Scholar
  12. Noack F (1986) NMR field-cycling spectroscopy: principles and applications. Prog NMR Spectrosc 18:171–276CrossRefGoogle Scholar
  13. Orekhov VY, Pervushin KV, Arseniev AS (1994) Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy. Eur J Biochem 219:887–896CrossRefPubMedGoogle Scholar
  14. Palmer AG 3rd (2014) Chemical exchange in biomacromolecules: past, present, and future. J Magn Reson 241:3–17CrossRefPubMedPubMedCentralGoogle Scholar
  15. Palmer AG, Massi F (2006) Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem Rev 106:1700–1719CrossRefPubMedGoogle Scholar
  16. Szyperski S, Luginbühl P, Otting G, Güntert P, Wüthrich K (1993) Protein dynamics studied by rotating frame. J Biomol NMR 3:151–164PubMedGoogle Scholar
  17. Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE (2001) Slow dynamics in folded and unfolded states of an SH3 domain. J Am Chem Soc 123:11341–11352CrossRefPubMedGoogle Scholar

Copyright information

© European Biophysical Societies' Association (EBSA) 2018

Authors and Affiliations

  • John D. Persons
    • 1
  • Shahid N. Khan
    • 1
  • Rieko Ishima
    • 1
  1. 1.Department of Structural BiologyUniversity of Pittsburgh School of MedicinePittsburghUSA

Section editors and affiliations

  • Mitsu Ikura

There are no affiliations available