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...
References
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 118:911–912
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 101:198–201
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 104:266–275
Halle B, Denisov VP (1995) A new view of water dynamics in immobilized proteins. Biophys J 69:242–249
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 112:5898–5904
Ishima R (2014) CPMG relaxation dispersion. Methods Mol Biol 1084:29–49
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 257:1–7
Kimmich R (1979) Field cycling in NMR relaxation spectroscopy: applications in biological, chemical and polymer physics. Bull Magn Reson 1:195–218
Koenig SH, Schillinger WE (1969) Nuclear magnetic relaxation dispersion in protein solutions. J Biol Chem 244:3283–3289
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 41:442–451
Loria JP, Berlow RB, Watt ED (2008) Characterization of enzyme motions by solution NMR relaxation dispersion. Acc Chem Res 41:212–221
Noack F (1986) NMR field-cycling spectroscopy: principles and applications. Prog NMR Spectrosc 18:171–276
Orekhov VY, Pervushin KV, Arseniev AS (1994) Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy. Eur J Biochem 219:887–896
Palmer AG 3rd (2014) Chemical exchange in biomacromolecules: past, present, and future. J Magn Reson 241:3–17
Palmer AG, Massi F (2006) Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem Rev 106:1700–1719
Szyperski S, Luginbühl P, Otting G, Güntert P, Wüthrich K (1993) Protein dynamics studied by rotating frame. J Biomol NMR 3:151–164
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 123:11341–11352
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Section Editor information
Rights and permissions
Copyright information
© 2018 European Biophysical Societies' Association (EBSA)
About this entry
Cite this entry
Persons, J.D., Khan, S.N., Ishima, R. (2018). Relaxation Dispersion. In: Roberts, G., Watts, A. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-35943-9_342-1
Download citation
DOI: https://doi.org/10.1007/978-3-642-35943-9_342-1
Received:
Accepted:
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-35943-9
Online ISBN: 978-3-642-35943-9
eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences