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* <section begin=Baldwin14/>Baldwin A. (2014). An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange. ''J. Magn. Reson.'', '''244''', 114-124. (DOI: [http://dx.doi.org/10.1016/j.jmr.2014.02.023 10.1016/j.jmr.2014.02.023])<section end=Baldwin14/>
* <section begin=Bieri11/>Bieri, M., d'Auvergne, E., and Gooley, P. (2011). relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins. ''J. Biomol. NMR'', '''50''', 147-155. (DOI: [http://dx.doi.org/10.1007/s10858-011-9509-1 10.1007/s10858-011-9509-1])<section end=Bieri11/>
* <section begin=CarverRichards72/>Carver, J. P. and Richards, R. E. (1972). General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. ''J. Magn. Reson.'', '''6'''(1), 89-105. (DOI [http://dx.doi.org/10.1016/0022-2364(72)90090-X 10.1016/0022-2364(72)90090-X])<section end=CarverRichards72/>
* <section begin=Clore90/>Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. (1990). Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. ''J. Am. Chem. Soc.'', '''112'''(12), 4989-4991. (DOI [http://dx.doi.org/10.1021/ja00168a070 10.1021/ja00168a070])<section end=Clore90/>
* <section begin=dAuvergneGooley03/>d'Auvergne, E. J. and Gooley, P. R. (2003). The use of model selection in the model-free analysis of protein dynamics. ''J. Biomol. NMR'', '''25'''(1), 25-39. (DOI [http://dx.doi.org/10.1023/a:1021902006114 10.1023/a:1021902006114])<section end=dAuvergneGooley03/>
* <section begin=dAuvergneGooley06/>d'Auvergne, E. J. and Gooley, P. R. (2006). Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data. ''J. Biomol. NMR'', '''35'''(2), 117-135. (DOI [http://dx.doi.org/10.1007/s10858-006-9007-z 10.1007/s10858-006-9007-z])<section end=dAuvergneGooley06/>
* <section begin=dAuvergneGooley07/>d'Auvergne, E. J. and Gooley, P. R. (2007). Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm. ''Mol. BioSyst.'', '''3'''(7), 483–494. (DOI: [http://dx.doi.org/10.1039/b702202f 10.1039/b702202f])<section end=dAuvergneGooley07/>
* <section begin=dAuvergneGooley08a/>d'Auvergne, E. J. and Gooley, P. R. (20082008a). Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. ''J. Biomol. NMR'', '''40'''(2), 107-119. (DOI: [http://dx.doi.org/10.1007/s10858-007-9214-2 10.1007/s10858-007-9214-2])<section end=dAuvergneGooley08a/> * <section begin=dAuvergneGooley08b/>d'Auvergne, E. J. and Gooley, P. R. (20082008b). Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. ''J. Biomol. NMR'', '''40'''(2), 121-133. (DOI: [http://dx.doi.org/10.1007/s10858-007-9213-3 10.1007/s10858-007-9213-3])<section end=dAuvergneGooley08b/> * <section begin=dAuvergneGooley08c/>d'Auvergne, E. J. and Gooley, P. R. (20082008c). Optimisation of NMR dynamic models. ''J. Biomol. NMR'', '''40'''(2), 107-133. (DOI: [http://dx.doi.org/10.1007/s10858-007-9214-2 10.1007/s10858-007-9214-2], [http://dx.doi.org/10.1007/s10858-007-9213-3 10.1007/s10858-007-9213-3])<section end=dAuvergneGooley08c/>
* <section begin=Davis94/>Davis, D. G., Perlman, M. E., and London, R. E. (1994). Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods. ''J. Magn. Reson.'', '''104'''(3), 266-275. (DOI [http://dx.doi.org/10.1006/jmrb.1994.1084 10.1006/jmrb.1994.1084])<section end=Davis94/>
* <section begin=Fushman98/> Fushman, D., Tjandra, N., and Cowburn, D. (1998). Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution. ''J. Am. Chem. Soc.'', '''120'''(42), 10947-10952. (DOI: [http://dx.doi.org/10.1021/ja981686m 10.1021/ja981686m])<section end=Fushman98/>
* <section begin=IshimaTorchia99/>Ishima, R. and Torchia, D. A. (2005). Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters. ''J. Biomol. NMR'', '''32'''(1), 41-54. (DOI [http://dx.doi.org/10.1007/s10858-005-3593-z 10.1007/s10858-005-3593-z])<section end=IshimaTorchia99/>
* <section begin=LuzMeiboom63/>Luz, Z. and Meiboom, S. (1963). Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent. ''J. Chem. Phys.'', '''39'''(2), 366-370. (DOI [http://dx.doi.org/10.1063/1.1734254 10.1063/1.1734254])<section end=LuzMeiboom63/>
* <section begin=Meiboom61/>Meiboom, S. (1961). Nuclear magnetic resonance study of proton transfer in water. ''J. Chem. Phys.'', '''34'''(2), 375-388. (DOI [http://dx.doi.org/10.1063/1.1700960 10.1063/1.1700960]).<section end=Meiboom61/>
* <section begin=MiloushevPalmer05/>Miloushev, V. Z. and Palmer, 3rd, A. G. (2005). R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions. ''J. Magn. Reson.'', '''177'''(2), 221-227. (DOI [http://dx.doi.org/10.1016/j.jmr.2005.07.023 10.1016/j.jmr.2005.07.023])<section end=MiloushevPalmer05/>
* <section begin=MorinGagné09/>Morin, S. and Gagné, S. (2009). Simple tests for the validation of multiple field spin relaxation data. ''J. Biomol. NMR'', '''45''', 361-372. (DOI: [http://dx.doi.org/10.1007/s10858-009-9381-4 10.1007/s10858-009-9381-4])<section end=MorinGagné09/>
* <section begin=Morin14/>Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., Teilum, K., Gagné, S., Marion, D., Griesinger, C., Blackledge, M., and d'Auvergne, E. J. (2014). relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. ''Bioinformatics'', '''30'''(15), 2219-2220. (DOI [http://dx.doi.org/10.1093/bioinformatics/btu166 10.1093/bioinformatics/btu166])<section end=Morin14/>
* <section begin=Orekhov99/>Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S. (1999). H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitions. ''J. Biomol. NMR'', '''14'''(4), 345-356. (DOI: [http://dx.doi.org/10.1023/a:1008356809071 10.1023/a:1008356809071])<section end=Orekhov99/>
* <section begin=Schurr94/>Schurr, J. M., Babcock, H. P., and Fujimoto, B. S. (1994). A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. ''J. Magn. Reson. B'', '''105'''(3), 211-224. (DOI: [http://dx.doi.org/10.1006/jmrb.1994.1127 10.1006/jmrb.1994.1127])<section end=Schurr94/>
* <section begin=Tollinger01/>Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E. (2001). Slow dynamics in folded and unfolded states of an sh3 domain. ''J. Am. Chem. Soc.'', '''123'''(46), 11341-11352. (DOI [http://dx.doi.org/10.1021/ja011300z 10.1021/ja011300z])<section end=Tollinger01/>
* <section begin=TrottPalmer02/>Trott, O. and Palmer, 3rd, A. G. (2002). R1rho relaxation outside of the fast-exchange limit. ''J. Magn. Reson.'', '''154'''(1), 157-160. (DOI [http://dx.doi.org/10.1006/jmre.2001.2466 10.1006/jmre.2001.2466])<section end=TrottPalmer02/>
* <section begin=Trott03/>Trott, O., Abergel, D., and Palmer, A. (2003). An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange. ''Mol. Phys.'', '''101'''(6), 753-763. (DOI [http://dx.doi.org/10.1080/0026897021000054826 10.1080/0026897021000054826])<section end=Trott03/>
* <section begin=Tjandra95/>Tjandra, N., Wingfield, P., Stahl, S., and Bax, A. (1996). Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic. ''J. Biomol. NMR'', '''8'''(3), 273-284. (DOI: [http://dx.doi.org/10.1007/bf00410326 10.1007/bf00410326])<section end=Tjandra95/>