Trusted, Bureaucrats
4,228
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Changes
Shifted the year parameter in all references to its position in the {{citation}} template.
* <section begin=Bieri11/>{{citation
| authors = Bieri, M., d'Auvergne, E., and Gooley, P.
| title = relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins.
| journal = J. Biomol. NMR
| page_start = 147
| page_end = 155
| year = 2011
| doi = 10.1007/s10858-011-9509-1
}}<section end=Bieri11/>
* <section begin=CarverRichards72/>{{citation
| authors = Carver, J. P. and Richards, R. E.
| title = General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation.
| journal = J. Magn. Reson.
| page_start = 89
| page_end = 105
| year = 1972
| doi = 10.1016/0022-2364(72)90090-X
}}<section end=CarverRichards72/>
* <section begin=Clore90/>{{citation
| authors = Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M.
| title = Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins.
| journal = J. Am. Chem. Soc.
| page_start = 4989
| page_end = 4991
| year = 1990
| doi = 10.1021/ja00168a070
}}<section end=Clore90/>
* <section begin=dAuvergneGooley03/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
| title = The use of model selection in the model-free analysis of protein dynamics.
| journal = J. Biomol. NMR
| page_start = 25
| page_end = 39
| year = 2003
| doi = 10.1023/a:1021902006114
}}<section end=dAuvergneGooley03/>
* <section begin=dAuvergneGooley06/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
| title = Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data.
| journal = J. Biomol. NMR
| page_start = 117
| page_end = 135
| year = 2006
| doi = 10.1007/s10858-006-9007-z
}}<section end=dAuvergneGooley06/>
* <section begin=dAuvergneGooley07/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
| title = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm.
| journal = Mol. BioSyst.
| page_start = 483
| page_end = 494
| year = 2007
| doi = 10.1039/b702202f
}}<section end=dAuvergneGooley07/>
* <section begin=dAuvergneGooley08a/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
| title = Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces.
| journal = J. Biomol. NMR
| page_start = 107
| page_end = 119
| year = 2008
| doi = 10.1007/s10858-007-9214-2
}}<section end=dAuvergneGooley08a/>
* <section begin=dAuvergneGooley08b/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
| title = Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor.
| journal = J. Biomol. NMR
| page_start = 121
| page_end = 133
| year = 2008
| doi = 10.1007/s10858-007-9213-3
}}<section end=dAuvergneGooley08b/>
* <section begin=dAuvergneGooley08c/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
| title = Optimisation of NMR dynamic models.
| journal = J. Biomol. NMR
| page_start = 107
| page_end = 133
| year = 2008
| doi = 10.1007/s10858-007-9214-2
| doi2 = 10.1007/s10858-007-9213-3
* <section begin=Davis94/>{{citation
| authors = Davis, D. G., Perlman, M. E., and London, R. E.
| title = Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods.
| journal = J. Magn. Reson.
| page_start = 266
| page_end = 275
| year = 1994
| doi = 10.1006/jmrb.1994.1084
}}<section end=Davis94/>
* <section begin=Farrow94/>{{citation
| authors = Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., Kay, L. E.
| title = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
| journal = Biochemistry
| page_start = 5984
| page_end = 6003
| year = 1994
| doi = 10.1021/bi00185a040
}}<section end=Farrow94/>
* <section begin=Fushman98/>{{citation
| authors = Fushman, D., Tjandra, N., and Cowburn, D.
| title = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution.
| journal = J. Am. Chem. Soc.
| page_start = 10947
| page_end = 10952
| year = 1998
| doi = 10.1021/ja981686m
}}<section end=Fushman98/>
* <section begin=IshimaTorchia99/>{{citation
| authors = Ishima, R. and Torchia, D. A.
| title = Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution.
| journal = J. Biomol. NMR
| page_start = 369
| page_end = 372
| year = 1999
| doi = 10.1023/A:1008324025406
}}<section end=IshimaTorchia99/>
* <section begin=IshimaTorchia05/>{{citation
| authors = Ishima, R. and Torchia, D. A.
| title = Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters.
| journal = J. Biomol. NMR
| page_start = 41
| page_end = 54
| year = 2005
| doi = 10.1007/s10858-005-3593-z
}}<section end=IshimaTorchia99/>
* <section begin=Korzhnev04a/>{{citation
| authors = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E.
| title = Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme.
| journal = J. Am. Chem. Soc.
| page_start = 3964
| page_end = 3973
| year = 2004
| doi = 10.1021/ja039587i
}}<section end=Korzhnev04a/>
* <section begin=Korzhnev04b/>{{citation
| authors = Korzhnev, D. M., Kloiber, K., and Kay, L. E.
| title = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application.
| journal = J. Am. Chem. Soc.
| page_start = 7320
| page_end = 7329
| year = 2004
| doi = 10.1021/ja049968b
}}<section end=Korzhnev04b/>
* <section begin=Korzhnev05a/>{{citation
| authors = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E.
| title = Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant.
| journal = J. Am. Chem. Soc.
| page_start = 15602
| page_end = 15611
| year = 2005
| doi = 10.1021/ja054550e
}}<section end=Korzhnev05a/>
* <section begin=Korzhnev05b/>{{citation
| authors = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E.
| title = Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain.
| journal = J. Am. Chem. Soc.
| page_start = 713
| page_end = 721
| year = 2005
| doi = 10.1021/ja0446855
}}<section end=Korzhnev05b/>
* <section begin=LuzMeiboom63/>{{citation
| authors = Luz, Z. and Meiboom, S.
| title = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent.
| journal = J. Chem. Phys.
| page_start = 366
| page_end = 370
| year = 1963
| doi = 10.1063/1.1734254
}}<section end=LuzMeiboom63/>
* <section begin=Meiboom61/>{{citation
| authors = Meiboom, S.
| title = Nuclear magnetic resonance study of proton transfer in water.
| journal = J. Chem. Phys.
| page_start = 375
| page_end = 388
| year = 1961
| doi = 10.1063/1.1700960
}}<section end=Meiboom61/>
* <section begin=MiloushevPalmer05/>{{citation
| authors = Miloushev, V. Z. and Palmer, 3rd, A. G.
| title = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions.
| journal = J. Magn. Reson.
| page_start = 221
| page_end = 227
| year = 2005
| doi = 10.1016/j.jmr.2005.07.023
}}<section end=MiloushevPalmer05/>
* <section begin=MorinGagné09/>{{citation
| authors = Morin, S. and Gagné, S.
| title = Simple tests for the validation of multiple field spin relaxation data.
| journal = J. Biomol. NMR
| page_start = 361
| page_end = 372
| year = 2009
| doi = 10.1007/s10858-009-9381-4
}}<section end=MorinGagné09/>
* <section begin=Morin14/>{{citation
| authors = 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.
| title = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data.
| journal = Bioinformatics
| page_start = 2219
| page_end = 2220
| year = 2014
| doi = 10.1093/bioinformatics/btu166
}}<section end=Morin14/>
* <section begin=Orekhov99/>{{citation
| authors = Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S.
| title = H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitions.
| journal = J. Biomol. NMR
| page_start = 345
| page_end = 356
| year = 1999
| doi = 10.1023/a:1008356809071
}}<section end=Orekhov99/>
* <section begin=Palmer91/>{{citation
| authors = Palmer, 3rd, A. G., Rance, M., and Wright, P. E.
| title = Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy.
| journal = J. Am. Chem. Soc.
| page_start = 4371
| page_end = 4380
| year = 1991
| doi = 10.1021/ja00012a001
}}<section end=Palmer91/>
* <section begin=Schurr94/>{{citation
| authors = Schurr, J. M., Babcock, H. P., and Fujimoto, B. S.
| title = A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization.
| journal = J. Magn. Reson. B
| page_start = 211
| page_end = 224
| year = 1994
| doi = 10.1006/jmrb.1994.1127
}}<section end=Schurr94/>
* <section begin=Tollinger01/>{{citation
| authors = Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E.
| title = Slow dynamics in folded and unfolded states of an sh3 domain.
| journal = J. Am. Chem. Soc.
| page_start = 11341
| page_end = 11352
| year = 2001
| doi = 10.1021/ja011300z
}}<section end=Tollinger01/>
* <section begin=Trott03/>{{citation
| authors = Trott, O., Abergel, D., and Palmer, A.
| title = An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange.
| journal = Mol. Phys.
| page_start = 753
| page_end = 763
| year = 2003
| doi = 10.1080/0026897021000054826
}}<section end=Trott03/>
* <section begin=TrottPalmer02/>{{citation
| authors = Trott, O. and Palmer, 3rd, A. G.
| title = R1rho relaxation outside of the fast-exchange limit.
| journal = J. Magn. Reson.
| page_start = 157
| page_end = 160
| year = 2002
| doi = 10.1006/jmre.2001.2466
}}<section end=TrottPalmer02/>
* <section begin=Tjandra95/>{{citation
| authors = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A.
| title = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic.
| journal = J. Biomol. NMR
| page_start = 273
| page_end = 284
| year = 1996
| doi = 10.1007/bf00410326
}}<section end=Tjandra95/>