Difference between revisions of "Citations"

From relax wiki
Jump to navigation Jump to search
(Added the Palmer06 reference.)
 
(18 intermediate revisions by the same user not shown)
Line 1: Line 1:
 
The following is an alphabetical list of all citations used on the relax wiki:
 
The following is an alphabetical list of all citations used on the relax wiki:
 +
 +
* <section begin=Bain11/>{{citation
 +
| authors    = Bain, A. D., Anand, C. A., and Nie, Z.
 +
| title      = Exact solution of the CPMG pulse sequence with phase variation down the echo train: Application to R2 measurements
 +
| journal    = J. Magn. Reson.
 +
| volume    = 209
 +
| issue      = 2
 +
| page_start = 183
 +
| page_end  = 194
 +
| year      = 2011
 +
| doi        = 10.1016/j.jmr.2011.01.009
 +
}}<section end=Bain11/>
  
 
* <section begin=Baldwin14/>{{citation
 
* <section begin=Baldwin14/>{{citation
Line 14: Line 26:
 
* <section begin=Bieri11/>{{citation
 
* <section begin=Bieri11/>{{citation
 
| authors    = Bieri, M., d'Auvergne, E., and Gooley, P.
 
| authors    = Bieri, M., d'Auvergne, E., and Gooley, P.
−
| year      = 2011
 
 
| title      = relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins.
 
| 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
 
| journal    = J. Biomol. NMR
Line 20: Line 31:
 
| page_start = 147
 
| page_start = 147
 
| page_end  = 155
 
| page_end  = 155
 +
| year      = 2011
 
| doi        = 10.1007/s10858-011-9509-1
 
| doi        = 10.1007/s10858-011-9509-1
 
}}<section end=Bieri11/>
 
}}<section end=Bieri11/>
 +
 +
* <section begin=BieriGooley11/>{{citation
 +
| authors    = Bieri, M. and Gooley, P.
 +
| title      = Automated NMR relaxation dispersion data analysis using NESSY.
 +
| journal    = BMC Bioinformatics
 +
| volume    = 12
 +
| page_start = 1
 +
| page_end  = 10
 +
| year      = 2011
 +
| doi        = 10.1186/1471-2105-12-421
 +
}}<section end=BieriGooley11/>
  
 
* <section begin=CarverRichards72/>{{citation
 
* <section begin=CarverRichards72/>{{citation
 
| authors    = Carver, J. P. and Richards, R. E.
 
| authors    = Carver, J. P. and Richards, R. E.
−
| year      = 1972
 
 
| title      = General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation.
 
| title      = General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation.
 
| journal    = J. Magn. Reson.
 
| journal    = J. Magn. Reson.
 
| volume    = 6
 
| volume    = 6
−
| number    = 1
+
| issue      = 1
 
| page_start = 89
 
| page_start = 89
 
| page_end  = 105
 
| page_end  = 105
 +
| year      = 1972
 
| doi        = 10.1016/0022-2364(72)90090-X
 
| doi        = 10.1016/0022-2364(72)90090-X
 
}}<section end=CarverRichards72/>
 
}}<section end=CarverRichards72/>
Line 37: Line 60:
 
* <section begin=Clore90/>{{citation
 
* <section begin=Clore90/>{{citation
 
| authors    = Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M.
 
| authors    = Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M.
−
| year      = 1990
 
 
| title      = Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins.
 
| 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.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 112
 
| volume    = 112
−
| number    = 12
+
| issue      = 12
 
| page_start = 4989
 
| page_start = 4989
 
| page_end  = 4991
 
| page_end  = 4991
 +
| year      = 1990
 
| doi        = 10.1021/ja00168a070
 
| doi        = 10.1021/ja00168a070
 
}}<section end=Clore90/>
 
}}<section end=Clore90/>
 +
 +
* <section begin=dAuvergne06/>{{citation_thesis
 +
| author    = d'Auvergne, E. J.
 +
| title      = Protein dynamics: a study of the model-free analysis of NMR relaxation data.
 +
| type      = PhD
 +
| department = Biochemistry and Molecular Biology
 +
| university = University of Melbourne
 +
| year      = 2006
 +
| link      = https://minerva-access.unimelb.edu.au/handle/11343/39174
 +
| pdf        = https://minerva-access.unimelb.edu.au/bitstream/handle/11343/39174/67077_00002799_01_thesis.pdf?sequence=1
 +
}}<section end=dAuvergne06/>
  
 
* <section begin=dAuvergneGooley03/>{{citation
 
* <section begin=dAuvergneGooley03/>{{citation
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
−
| year      = 2003
 
 
| title      = The use of model selection in the model-free analysis of protein dynamics.
 
| title      = The use of model selection in the model-free analysis of protein dynamics.
 
| journal    = J. Biomol. NMR
 
| journal    = J. Biomol. NMR
 
| volume    = 25
 
| volume    = 25
−
| number    = 1
+
| issue      = 1
 
| page_start = 25
 
| page_start = 25
 
| page_end  = 39
 
| page_end  = 39
 +
| year      = 2003
 
| doi        = 10.1023/a:1021902006114
 
| doi        = 10.1023/a:1021902006114
 
}}<section end=dAuvergneGooley03/>
 
}}<section end=dAuvergneGooley03/>
Line 61: Line 95:
 
* <section begin=dAuvergneGooley06/>{{citation
 
* <section begin=dAuvergneGooley06/>{{citation
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
−
| year      = 2006
 
 
| title      = Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data.
 
| title      = Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data.
 
| journal    = J. Biomol. NMR
 
| journal    = J. Biomol. NMR
 
| volume    = 35
 
| volume    = 35
−
| number    = 2
+
| issue      = 2
 
| page_start = 117
 
| page_start = 117
 
| page_end  = 135
 
| page_end  = 135
 +
| year      = 2006
 
| doi        = 10.1007/s10858-006-9007-z
 
| doi        = 10.1007/s10858-006-9007-z
 
}}<section end=dAuvergneGooley06/>
 
}}<section end=dAuvergneGooley06/>
Line 73: Line 107:
 
* <section begin=dAuvergneGooley07/>{{citation
 
* <section begin=dAuvergneGooley07/>{{citation
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
−
| year      = 2007
 
 
| title      = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm.
 
| title      = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm.
 
| journal    = Mol. BioSyst.
 
| journal    = Mol. BioSyst.
 
| volume    = 3
 
| volume    = 3
−
| number    = 7
+
| issue      = 7
 
| page_start = 483
 
| page_start = 483
 
| page_end  = 494
 
| page_end  = 494
 +
| year      = 2007
 
| doi        = 10.1039/b702202f
 
| doi        = 10.1039/b702202f
 
}}<section end=dAuvergneGooley07/>
 
}}<section end=dAuvergneGooley07/>
Line 85: Line 119:
 
* <section begin=dAuvergneGooley08a/>{{citation
 
* <section begin=dAuvergneGooley08a/>{{citation
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
−
| year      = 2008a
 
 
| title      =  Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces.
 
| 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
 
| journal    = J. Biomol. NMR
 
| volume    = 40
 
| volume    = 40
−
| number    = 2
+
| issue      = 2
 
| page_start = 107
 
| page_start = 107
 
| page_end  = 119
 
| page_end  = 119
 +
| year      = 2008
 
| doi        = 10.1007/s10858-007-9214-2
 
| doi        = 10.1007/s10858-007-9214-2
 
}}<section end=dAuvergneGooley08a/>
 
}}<section end=dAuvergneGooley08a/>
Line 97: Line 131:
 
* <section begin=dAuvergneGooley08b/>{{citation
 
* <section begin=dAuvergneGooley08b/>{{citation
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
−
| year      = 2008b
 
 
| 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.
 
| 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
 
| journal    = J. Biomol. NMR
 
| volume    = 40
 
| volume    = 40
−
| number    = 2
+
| issue      = 2
 
| page_start = 121
 
| page_start = 121
 
| page_end  = 133
 
| page_end  = 133
 +
| year      = 2008
 
| doi        = 10.1007/s10858-007-9213-3
 
| doi        = 10.1007/s10858-007-9213-3
 
}}<section end=dAuvergneGooley08b/>
 
}}<section end=dAuvergneGooley08b/>
Line 109: Line 143:
 
* <section begin=dAuvergneGooley08c/>{{citation
 
* <section begin=dAuvergneGooley08c/>{{citation
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 
| authors    = d'Auvergne, E. J. and Gooley, P. R.
−
| year      = 2008c
 
 
| title      = Optimisation of NMR dynamic models.
 
| title      = Optimisation of NMR dynamic models.
 
| journal    = J. Biomol. NMR
 
| journal    = J. Biomol. NMR
 
| volume    = 40
 
| volume    = 40
−
| number    = 2
+
| issue      = 2
 
| page_start = 107
 
| page_start = 107
 
| page_end  = 133
 
| page_end  = 133
 +
| year      = 2008
 
| doi        = 10.1007/s10858-007-9214-2
 
| doi        = 10.1007/s10858-007-9214-2
 
| doi2      = 10.1007/s10858-007-9213-3
 
| doi2      = 10.1007/s10858-007-9213-3
Line 122: Line 156:
 
* <section begin=Davis94/>{{citation
 
* <section begin=Davis94/>{{citation
 
| authors    = Davis, D. G., Perlman, M. E., and London, R. E.
 
| authors    = Davis, D. G., Perlman, M. E., and London, R. E.
−
| year      = 1994
 
 
| title      = Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods.
 
| title      = Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods.
 
| journal    = J. Magn. Reson.
 
| journal    = J. Magn. Reson.
 
| volume    = 104
 
| volume    = 104
−
| number    = 3
+
| issue      = 3
 
| page_start = 266
 
| page_start = 266
 
| page_end  = 275
 
| page_end  = 275
 +
| year      = 1994
 
| doi        = 10.1006/jmrb.1994.1084
 
| doi        = 10.1006/jmrb.1994.1084
 
}}<section end=Davis94/>
 
}}<section end=Davis94/>
 +
 +
* <section begin=Erdelyi11/>{{citation
 +
| authors    = Erdélyi, M., d'Auvergne, E., Navarro-Vázquez, A., Leonov, A., and Griesinger, C.
 +
| title      = Dynamics of the glycosidic bond: conformational space of lactose.
 +
| journal    = Chem. Eur. J.
 +
| volume    = 17
 +
| issue      = 34
 +
| page_start = 9368
 +
| page_end  = 9376
 +
| year      = 2011
 +
| doi        = 10.1002/chem.201100854
 +
}}<section end=Erdelyi11/>
 +
 +
* <section begin=Evenäs01/>{{citation
 +
| authors    = Evenäs, J., Malmendal, A. and Akke, M.
 +
| title      = Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.
 +
| journal    = Structure
 +
| volume    = 9
 +
| issue      = 3
 +
| page_start = 185
 +
| page_end  = 195
 +
| year      = 2001
 +
| doi        = 10.1016/S0969-2126(01)00575-5
 +
}}<section end=Evenäs01/>
  
 
* <section begin=Farrow94/>{{citation
 
* <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.
 
| 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.
−
| year      = 1994
 
 
| title      = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
 
| title      = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
 
| journal    = Biochemistry
 
| journal    = Biochemistry
 
| volume    = 33
 
| volume    = 33
−
| number    = 19
+
| issue      = 19
 
| page_start = 5984
 
| page_start = 5984
 
| page_end  = 6003
 
| page_end  = 6003
 +
| year      = 1994
 
| doi        = 10.1021/bi00185a040
 
| doi        = 10.1021/bi00185a040
 
}}<section end=Farrow94/>
 
}}<section end=Farrow94/>
Line 146: Line 204:
 
* <section begin=Fushman98/>{{citation
 
* <section begin=Fushman98/>{{citation
 
| authors    = Fushman, D., Tjandra, N., and Cowburn, D.
 
| authors    = Fushman, D., Tjandra, N., and Cowburn, D.
−
| year      = 1998
 
 
| title      = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution.
 
| title      = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution.
 
| journal    = J. Am. Chem. Soc.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 120
 
| volume    = 120
−
| number    = 42
+
| issue      = 42
 
| page_start = 10947
 
| page_start = 10947
 
| page_end  = 10952
 
| page_end  = 10952
 +
| year      = 1998
 
| doi        = 10.1021/ja981686m
 
| doi        = 10.1021/ja981686m
 
}}<section end=Fushman98/>
 
}}<section end=Fushman98/>
 +
 +
* <section begin=Fushman99/>{{citation
 +
| authors    = Fushman, D., Tjandra, N., and Cowburn, D.
 +
| title      = An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 121
 +
| issue      = 37
 +
| page_start = 8577
 +
| page_end  = 8582
 +
| year      = 1999
 +
| doi        = 10.1021/ja9904991
 +
}}<section end=Fushman99/>
 +
 +
* <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
 +
| volume    = 14
 +
| issue      = 4
 +
| 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
 +
| volume    = 32
 +
| issue      = 1
 +
| page_start = 41
 +
| page_end  = 54
 +
| year      = 2005
 +
| doi        = 10.1007/s10858-005-3593-z
 +
}}<section end=IshimaTorchia99/>
 +
 +
* <section begin=KempfLoria04/>{{citation
 +
| authors    = Kempf, J. G. and Loria, J. P.
 +
| title      = Measurement of intermediate exchange phenomena.
 +
| journal    = Methods Mol. Biol.
 +
| volume    = 278
 +
| page_start = 185
 +
| page_end  = 231
 +
| year      = 2004
 +
| doi        = 10.1385/1-59259-809-9:185
 +
}}<section end=KempfLoria04/>
  
 
* <section begin=Korzhnev04a/>{{citation
 
* <section begin=Korzhnev04a/>{{citation
 
| authors    = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E.
 
| authors    = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E.
−
| year      = 2004
 
 
| title      = Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme.
 
| 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.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 126
 
| volume    = 126
−
| number    = 12
+
| issue      = 12
 
| page_start = 3964
 
| page_start = 3964
 
| page_end  = 3973
 
| page_end  = 3973
 +
| year      = 2004
 
| doi        = 10.1021/ja039587i
 
| doi        = 10.1021/ja039587i
 
}}<section end=Korzhnev04a/>
 
}}<section end=Korzhnev04a/>
Line 170: Line 275:
 
* <section begin=Korzhnev04b/>{{citation
 
* <section begin=Korzhnev04b/>{{citation
 
| authors    = Korzhnev, D. M., Kloiber, K., and Kay, L. E.
 
| authors    = Korzhnev, D. M., Kloiber, K., and Kay, L. E.
−
| year      = 2004
 
 
| title      = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application.
 
| title      = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application.
 
| journal    = J. Am. Chem. Soc.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 126
 
| volume    = 126
−
| number    = 23
+
| issue      = 23
 
| page_start = 7320
 
| page_start = 7320
 
| page_end  = 7329
 
| page_end  = 7329
 +
| year      = 2004
 
| doi        = 10.1021/ja049968b
 
| doi        = 10.1021/ja049968b
 
}}<section end=Korzhnev04b/>
 
}}<section end=Korzhnev04b/>
Line 182: Line 287:
 
* <section begin=Korzhnev05a/>{{citation
 
* <section begin=Korzhnev05a/>{{citation
 
| authors    = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E.
 
| authors    = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E.
−
| year      = 2005
 
 
| 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.
 
| 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.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 127
 
| volume    = 127
−
| number    = 44
+
| issue      = 44
 
| page_start = 15602
 
| page_start = 15602
 
| page_end  = 15611
 
| page_end  = 15611
 +
| year      = 2005
 
| doi        = 10.1021/ja054550e
 
| doi        = 10.1021/ja054550e
 
}}<section end=Korzhnev05a/>
 
}}<section end=Korzhnev05a/>
Line 194: Line 299:
 
* <section begin=Korzhnev05b/>{{citation
 
* <section begin=Korzhnev05b/>{{citation
 
| authors    = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E.
 
| authors    = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E.
−
| year      = 2005
 
 
| title      = Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain.
 
| 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.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 127
 
| volume    = 127
−
| number    = 2
+
| issue      = 2
 
| page_start = 713
 
| page_start = 713
 
| page_end  = 721
 
| page_end  = 721
 +
| year      = 2005
 
| doi        = 10.1021/ja0446855
 
| doi        = 10.1021/ja0446855
 
}}<section end=Korzhnev05b/>
 
}}<section end=Korzhnev05b/>
  
−
* <section begin=IshimaTorchia99/>{{citation
+
* <section begin=LipariSzabo82a/>{{citation
−
| authors    = Ishima, R. and Torchia, D. A.
+
| authors    = Lipari, G. and Szabo, A.
−
| year      = 2005
+
| title      = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules I. Theory and range of validity.
−
| title      = Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters.
+
| journal    = J. Am. Chem. Soc.
−
| journal    = J. Biomol. NMR
+
| volume    = 104
−
| volume    = 32
+
| issue      = 17
−
| number    = 1
+
| page_start = 4546
−
| page_start = 41
+
| page_end  = 4559
−
| page_end  = 54
+
| year      = 1982
−
| doi        = 10.1007/s10858-005-3593-z
+
| doi        = 10.1021/ja00381a009
−
}}<section end=IshimaTorchia99/>
+
}}<section end=LipariSzabo82a/>
 +
 
 +
* <section begin=LipariSzabo82b/>{{citation
 +
| authors    = Lipari, G. and Szabo, A.
 +
| title      = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules II. Analysis of experimental results.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 104
 +
| issue      = 17
 +
| page_start = 4559
 +
| page_end  = 4570
 +
| year      = 1982
 +
| doi        = 10.1021/ja00381a010
 +
}}<section end=LipariSzabo82b/>
  
 
* <section begin=LuzMeiboom63/>{{citation
 
* <section begin=LuzMeiboom63/>{{citation
 
| authors    = Luz, Z. and Meiboom, S.
 
| authors    = Luz, Z. and Meiboom, S.
−
| year      = 1963
 
 
| title      = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent.
 
| title      = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent.
 
| journal    = J. Chem. Phys.
 
| journal    = J. Chem. Phys.
 
| volume    = 39
 
| volume    = 39
−
| number    = 2
+
| issue      = 2
 
| page_start = 366
 
| page_start = 366
 
| page_end  = 370
 
| page_end  = 370
 +
| year      = 1963
 
| doi        = 10.1063/1.1734254
 
| doi        = 10.1063/1.1734254
 
}}<section end=LuzMeiboom63/>
 
}}<section end=LuzMeiboom63/>
 +
 +
* <section begin=Mandel95/>{{citation
 +
| authors    = Mandel, A. M., Akke, M., and Palmer, 3rd, A. G.
 +
| title      = Backbone dynamics of ''Escherichia coli'' ribonuclease HI: correlations with structure and function in an active enzyme.
 +
| journal    = J. Mol. Biol.
 +
| volume    = 246
 +
| issue      = 1
 +
| page_start = 144
 +
| page_end  = 163
 +
| year      = 1995
 +
| doi        = 10.1006/jmbi.1994.0073
 +
}}<section end=Mandel95/>
 +
 +
* <section begin=Massi05/>{{citation
 +
| authors    = Massi, F., Grey, M. J., Palmer, 3rd, A. G.
 +
| title      = Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments
 +
| journal    = Protein science
 +
| volume    = 14
 +
| issue      = 3
 +
| page_start = 735
 +
| page_end  = 742
 +
| year      = 2005
 +
| doi        = 10.1110/ps.041139505
 +
}}<section end=Massi05/>
  
 
* <section begin=Meiboom61/>{{citation
 
* <section begin=Meiboom61/>{{citation
 
| authors    = Meiboom, S.
 
| authors    = Meiboom, S.
−
| year      = 1961
 
 
| title      = Nuclear magnetic resonance study of proton transfer in water.
 
| title      = Nuclear magnetic resonance study of proton transfer in water.
 
| journal    = J. Chem. Phys.
 
| journal    = J. Chem. Phys.
 
| volume    = 34
 
| volume    = 34
−
| number    = 2
+
| issue      = 2
 
| page_start = 375
 
| page_start = 375
 
| page_end  = 388
 
| page_end  = 388
 +
| year      = 1961
 
| doi        = 10.1063/1.1700960
 
| doi        = 10.1063/1.1700960
 
}}<section end=Meiboom61/>
 
}}<section end=Meiboom61/>
Line 242: Line 383:
 
* <section begin=MiloushevPalmer05/>{{citation
 
* <section begin=MiloushevPalmer05/>{{citation
 
| authors    = Miloushev, V. Z. and Palmer, 3rd, A. G.
 
| authors    = Miloushev, V. Z. and Palmer, 3rd, A. G.
−
| year      = 2005
 
 
| title      = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions.
 
| title      = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions.
 
| journal    = J. Magn. Reson.
 
| journal    = J. Magn. Reson.
 
| volume    = 177
 
| volume    = 177
−
| number    = 2
+
| issue      = 2
 
| page_start = 221
 
| page_start = 221
 
| page_end  = 227
 
| page_end  = 227
 +
| year      = 2005
 
| doi        = 10.1016/j.jmr.2005.07.023
 
| doi        = 10.1016/j.jmr.2005.07.023
 
}}<section end=MiloushevPalmer05/>
 
}}<section end=MiloushevPalmer05/>
Line 254: Line 395:
 
* <section begin=MorinGagné09/>{{citation
 
* <section begin=MorinGagné09/>{{citation
 
| authors    = Morin, S. and Gagné, S.
 
| authors    = Morin, S. and Gagné, S.
−
| year      = 2009
 
 
| title      = Simple tests for the validation of multiple field spin relaxation data.
 
| title      = Simple tests for the validation of multiple field spin relaxation data.
 
| journal    = J. Biomol. NMR
 
| journal    = J. Biomol. NMR
Line 260: Line 400:
 
| page_start = 361
 
| page_start = 361
 
| page_end  = 372
 
| page_end  = 372
 +
| year      = 2009
 
| doi        = 10.1007/s10858-009-9381-4
 
| doi        = 10.1007/s10858-009-9381-4
 
}}<section end=MorinGagné09/>
 
}}<section end=MorinGagné09/>
Line 265: Line 406:
 
* <section begin=Morin14/>{{citation
 
* <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.
 
| 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.
−
| year      = 2014
 
 
| title      = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data.
 
| title      = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data.
 
| journal    = Bioinformatics
 
| journal    = Bioinformatics
 
| volume    = 30
 
| volume    = 30
−
| number    = 15
+
| issue      = 15
 
| page_start = 2219
 
| page_start = 2219
 
| page_end  = 2220
 
| page_end  = 2220
 +
| year      = 2014
 
| doi        = 10.1093/bioinformatics/btu166
 
| doi        = 10.1093/bioinformatics/btu166
 
}}<section end=Morin14/>
 
}}<section end=Morin14/>
 +
 +
* <section begin=MyintIshima09/>{{citation
 +
| authors    = Myint, W. and Ishima, R.
 +
| title      = Chemical exchange effects during refocusing pulses in constant-time CPMG relaxation dispersion experiments
 +
| journal    = J. Biomol. NMR
 +
| volume    = 45
 +
| issue      = 1
 +
| page_start = 207
 +
| page_end  = 216
 +
| year      = 2009
 +
| doi        = 10.1007/s10858-009-9344-9
 +
}}<section end=MyintIshima09/>
 +
 +
* <section begin=Orekhov95/>{{citation
 +
| authors    = Orekhov, V. Y., Nolde, D. E., Golovanov, A. P., Korzhnev, D. M. and Arseniev, A. S.
 +
| title      = Processing of heteronuclear NMR relaxation data with the new software DASHA
 +
| journal    = Appl. Magn. Reson.
 +
| volume    = 9
 +
| issue      = 4
 +
| page_start = 581
 +
| page_end  = 588
 +
| year      = 1995
 +
| doi        = 10.1007/bf03162365
 +
}}<section end=Orekhov95/>
  
 
* <section begin=Orekhov99/>{{citation
 
* <section begin=Orekhov99/>{{citation
 
| authors    = Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S.
 
| authors    = Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S.
−
| year      = 1999
 
 
| title      = H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitions.
 
| 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
 
| journal    = J. Biomol. NMR
 
| volume    = 14
 
| volume    = 14
−
| number    = 4
+
| issue      = 4
 
| page_start = 345
 
| page_start = 345
 
| page_end  = 356
 
| page_end  = 356
 +
| year      = 1999
 
| doi        = 10.1023/a:1008356809071
 
| doi        = 10.1023/a:1008356809071
 
}}<section end=Orekhov99/>
 
}}<section end=Orekhov99/>
 +
 +
* <section begin=Palmer01/>{{citation
 +
| authors    = Palmer, 3rd, A. G., Kroenke, C. D., and Loria, J. P.
 +
| title      = Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules.
 +
| journal    = Methods Enzymol.
 +
| volume    = 339
 +
| page_start = 204
 +
| page_end  = 238
 +
| year      = 2001
 +
| doi        = 10.1016/S0076-6879(01)39315-1
 +
}}<section end=Palmer01/>
 +
 +
* <section begin=PalmerMassi06/>{{citation
 +
| authors    = Palmer, 3rd, A. G. and Massi, F.
 +
| title      = Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy.
 +
| journal    = Chem. Rev.
 +
| volume    = 106
 +
| issue      = 5
 +
| page_start = 1700
 +
| page_end  = 1719
 +
| year      = 2006
 +
| doi        = 10.1021/cr0404287
 +
}}<section end=PalmerMassi06/>
  
 
* <section begin=Palmer91/>{{citation
 
* <section begin=Palmer91/>{{citation
 
| authors    = Palmer, 3rd, A. G., Rance, M., and Wright, P. E.
 
| authors    = Palmer, 3rd, A. G., Rance, M., and Wright, P. E.
−
| year      = 1991
 
 
| title      = Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy.
 
| 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.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 113
 
| volume    = 113
−
| number    = 12
+
| issue      = 12
 
| page_start = 4371
 
| page_start = 4371
 
| page_end  = 4380
 
| page_end  = 4380
 +
| year      = 1991
 
| doi        = 10.1021/ja00012a001
 
| doi        = 10.1021/ja00012a001
 
}}<section end=Palmer91/>
 
}}<section end=Palmer91/>
−
 
−
* <section begin=Palmer06/>{{citation
 
−
| authors    = Palmer, 3rd, A. G. and Massi, F.
 
−
| title      = Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy.
 
−
| journal    = Chem. Rev.
 
−
| volume    = 106
 
−
| number    = 5
 
−
| page_start = 1700
 
−
| page_end  = 1719
 
−
| year      = 2006
 
−
| doi        = 10.1021/cr0404287
 
−
}}<section end=Palmer06/>
 
  
 
* <section begin=Schurr94/>{{citation
 
* <section begin=Schurr94/>{{citation
 
| authors    = Schurr, J. M., Babcock, H. P., and Fujimoto, B. S.
 
| authors    = Schurr, J. M., Babcock, H. P., and Fujimoto, B. S.
−
| year      = 1994
 
 
| title      = A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization.
 
| title      = A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization.
 
| journal    = J. Magn. Reson. B
 
| journal    = J. Magn. Reson. B
 
| volume    = 105
 
| volume    = 105
−
| number    = 3
+
| issue      = 3
 
| page_start = 211
 
| page_start = 211
 
| page_end  = 224
 
| page_end  = 224
 +
| year      = 1994
 
| doi        = 10.1006/jmrb.1994.1127
 
| doi        = 10.1006/jmrb.1994.1127
 
}}<section end=Schurr94/>
 
}}<section end=Schurr94/>
 +
 +
* <section begin=Sun11/>{{citation
 +
| authors    = Sun, H., d'Auvergne, E. J., Reinscheid, U. M., Dias, L. C., Andrade, C. K. Z., Rocha, R. O., and Griesinger, C.
 +
| title      = Bijvoet in solution reveals unexpected stereoselectivity in a michael addition.
 +
| journal    = Chem. Eur. J.
 +
| volume    = 17
 +
| issue      = 6
 +
| page_start = 1811
 +
| page_end  = 1817
 +
| year      = 2011
 +
| doi        = 10.1002/chem.201002520
 +
}}<section end=Sun11/>
  
 
* <section begin=Tollinger01/>{{citation
 
* <section begin=Tollinger01/>{{citation
 
| authors    = Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E.
 
| authors    = Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E.
−
| year      = 2001
 
 
| title      = Slow dynamics in folded and unfolded states of an sh3 domain.
 
| title      = Slow dynamics in folded and unfolded states of an sh3 domain.
 
| journal    = J. Am. Chem. Soc.
 
| journal    = J. Am. Chem. Soc.
 
| volume    = 123
 
| volume    = 123
−
| number    = 46
+
| issue      = 46
 
| page_start = 11341
 
| page_start = 11341
 
| page_end  = 11352
 
| page_end  = 11352
 +
| year      = 2001
 
| doi        = 10.1021/ja011300z
 
| doi        = 10.1021/ja011300z
 
}}<section end=Tollinger01/>
 
}}<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.
 +
| volume    = 101
 +
| issue      = 6
 +
| page_start = 753
 +
| page_end  = 763
 +
| year      = 2003
 +
| doi        = 10.1080/0026897021000054826
 +
}}<section end=Trott03/>
  
 
* <section begin=TrottPalmer02/>{{citation
 
* <section begin=TrottPalmer02/>{{citation
 
| authors    = Trott, O. and Palmer, 3rd, A. G.
 
| authors    = Trott, O. and Palmer, 3rd, A. G.
−
| year      = 2002
 
 
| title      = R1rho relaxation outside of the fast-exchange limit.
 
| title      = R1rho relaxation outside of the fast-exchange limit.
 
| journal    = J. Magn. Reson.
 
| journal    = J. Magn. Reson.
 
| volume    = 154
 
| volume    = 154
−
| number    = 1
+
| issue      = 1
 
| page_start = 157
 
| page_start = 157
 
| page_end  = 160
 
| page_end  = 160
 +
| year      = 2002
 
| doi        = 10.1006/jmre.2001.2466
 
| doi        = 10.1006/jmre.2001.2466
 
}}<section end=TrottPalmer02/>
 
}}<section end=TrottPalmer02/>
−
 
−
* <section begin=Trott03/>{{citation
 
−
| authors    = Trott, O., Abergel, D., and Palmer, A.
 
−
| year      = 2003
 
−
| title      = An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange.
 
−
| journal    = Mol. Phys.
 
−
| volume    = 101
 
−
| number    = 6
 
−
| page_start = 753
 
−
| page_end  = 763
 
−
| doi        = 10.1080/0026897021000054826
 
−
}}<section end=Trott03/>
 
  
 
* <section begin=Tjandra95/>{{citation
 
* <section begin=Tjandra95/>{{citation
 
| authors    = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A.
 
| authors    = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A.
−
| year      = 1996
 
 
| title      = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic.
 
| title      = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic.
 
| journal    = J. Biomol. NMR
 
| journal    = J. Biomol. NMR
 
| volume    = 8
 
| volume    = 8
−
| number    = 3
+
| issue      = 3
 
| page_start = 273
 
| page_start = 273
 
| page_end  = 284
 
| page_end  = 284
 +
| year      = 1996
 
| doi        = 10.1007/bf00410326
 
| doi        = 10.1007/bf00410326
 
}}<section end=Tjandra95/>
 
}}<section end=Tjandra95/>
 +
 +
* <section begin=Vallurupalli08/>{{citation
 +
| authors    = Vallurupalli, P., Hansen, D. F., and Kay, L. E.
 +
| title      = Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
 +
| journal    = Proc. Natl. Acad. Sci. USA
 +
| volume    = 105
 +
| issue      = 33
 +
| page_start = 11766
 +
| page_end  = 11771
 +
| year      = 2008
 +
| doi        = 10.1073/pnas.0804221105
 +
}}<section end=Vallurupalli08/>
 +
 +
* <section begin=Vallurupalli07/>{{citation
 +
| authors    = Vallurupalli, P., Hansen, D. F., Stollar, E., Meirovitch, E. and Kay, L. E.
 +
| title      = Measurement of bond vector orientations in invisible excited states of proteins
 +
| journal    = Proc. Natl. Acad. Sci. USA
 +
| volume    = 104
 +
| issue      = 47
 +
| page_start = 18473
 +
| page_end  = 18477
 +
| year      = 2007
 +
| doi        = 10.1073/pnas.0708296104
 +
}}<section end=Vallurupalli07/>
 +
 +
[[Category:Documentation]]

Latest revision as of 21:52, 21 October 2020

The following is an alphabetical list of all citations used on the relax wiki:

  • Bain, A. D., Anand, C. A., and Nie, Z. (2011). Exact solution of the CPMG pulse sequence with phase variation down the echo train: Application to R2 measurements J. Magn. Reson., 209(2), 183-194. (DOI: 10.1016/j.jmr.2011.01.009)
  • Baldwin A. J. (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: 10.1016/j.jmr.2014.02.023)
  • 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: 10.1007/s10858-011-9509-1)
  • Bieri, M. and Gooley, P. (2011). Automated NMR relaxation dispersion data analysis using NESSY. BMC Bioinformatics, 12, 1-10. (DOI: 10.1186/1471-2105-12-421)
  • 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: 10.1016/0022-2364(72)90090-X)
  • 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: 10.1021/ja00168a070)
  • d'Auvergne, E. J. (2006). Protein dynamics: a study of the model-free analysis of NMR relaxation data. PhD thesis, Biochemistry and Molecular Biology, University of Melbourne. (Link, PDF)
  • 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: 10.1023/a:1021902006114)
  • 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: 10.1007/s10858-006-9007-z)
  • 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: 10.1039/b702202f)
  • d'Auvergne, E. J. and Gooley, P. R. (2008). 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: 10.1007/s10858-007-9214-2)
  • d'Auvergne, E. J. and Gooley, P. R. (2008). 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: 10.1007/s10858-007-9213-3)
  • 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: 10.1006/jmrb.1994.1084)
  • Erdélyi, M., d'Auvergne, E., Navarro-Vázquez, A., Leonov, A., and Griesinger, C. (2011). Dynamics of the glycosidic bond: conformational space of lactose. Chem. Eur. J., 17(34), 9368-9376. (DOI: 10.1002/chem.201100854)
  • Evenäs, J., Malmendal, A. and Akke, M. (2001). Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant. Structure, 9(3), 185-195. (DOI: 10.1016/S0969-2126(01)00575-5)
  • 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. (1994). Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry, 33(19), 5984-6003. (DOI: 10.1021/bi00185a040)
  • Fushman, D., Tjandra, N., and Cowburn, D. (1998). Direct measurement of 15N chemical shift anisotropy in solution. J. Am. Chem. Soc., 120(42), 10947-10952. (DOI: 10.1021/ja981686m)
  • Fushman, D., Tjandra, N., and Cowburn, D. (1999). An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions. J. Am. Chem. Soc., 121(37), 8577-8582. (DOI: 10.1021/ja9904991)
  • Ishima, R. and Torchia, D. A. (1999). Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. J. Biomol. NMR, 14(4), 369-372. (DOI: 10.1023/A:1008324025406)
  • 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: 10.1007/s10858-005-3593-z)
  • Kempf, J. G. and Loria, J. P. (2004). Measurement of intermediate exchange phenomena. Methods Mol. Biol., 278, 185-231. (DOI: 10.1385/1-59259-809-9:185)
  • Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E. (2004). Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. J. Am. Chem. Soc., 126(12), 3964-3973. (DOI: 10.1021/ja039587i)
  • Korzhnev, D. M., Kloiber, K., and Kay, L. E. (2004). Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application. J. Am. Chem. Soc., 126(23), 7320-7329. (DOI: 10.1021/ja049968b)
  • Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E. (2005). 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. J. Am. Chem. Soc., 127(44), 15602-15611. (DOI: 10.1021/ja054550e)
  • Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E. (2005). Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. J. Am. Chem. Soc., 127(2), 713-721. (DOI: 10.1021/ja0446855)
  • Lipari, G. and Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules I. Theory and range of validity. J. Am. Chem. Soc., 104(17), 4546-4559. (DOI: 10.1021/ja00381a009)
  • Lipari, G. and Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules II. Analysis of experimental results. J. Am. Chem. Soc., 104(17), 4559-4570. (DOI: 10.1021/ja00381a010)
  • 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: 10.1063/1.1734254)
  • Mandel, A. M., Akke, M., and Palmer, 3rd, A. G. (1995). Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol., 246(1), 144-163. (DOI: 10.1006/jmbi.1994.0073)
  • Massi, F., Grey, M. J., Palmer, 3rd, A. G. (2005). Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments Protein science, 14(3), 735-742. (DOI: 10.1110/ps.041139505)
  • Meiboom, S. (1961). Nuclear magnetic resonance study of proton transfer in water. J. Chem. Phys., 34(2), 375-388. (DOI: 10.1063/1.1700960)
  • 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: 10.1016/j.jmr.2005.07.023)
  • Morin, S. and Gagné, S. (2009). Simple tests for the validation of multiple field spin relaxation data. J. Biomol. NMR, 45, 361-372. (DOI: 10.1007/s10858-009-9381-4)
  • 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: 10.1093/bioinformatics/btu166)
  • Myint, W. and Ishima, R. (2009). Chemical exchange effects during refocusing pulses in constant-time CPMG relaxation dispersion experiments J. Biomol. NMR, 45(1), 207-216. (DOI: 10.1007/s10858-009-9344-9)
  • Orekhov, V. Y., Nolde, D. E., Golovanov, A. P., Korzhnev, D. M. and Arseniev, A. S. (1995). Processing of heteronuclear NMR relaxation data with the new software DASHA Appl. Magn. Reson., 9(4), 581-588. (DOI: 10.1007/bf03162365)
  • 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: 10.1023/a:1008356809071)
  • Palmer, 3rd, A. G., Kroenke, C. D., and Loria, J. P. (2001). Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol., 339, 204-238. (DOI: 10.1016/S0076-6879(01)39315-1)
  • Palmer, 3rd, A. G. and Massi, F. (2006). Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem. Rev., 106(5), 1700-1719. (DOI: 10.1021/cr0404287)
  • Palmer, 3rd, A. G., Rance, M., and Wright, P. E. (1991). Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. J. Am. Chem. Soc., 113(12), 4371-4380. (DOI: 10.1021/ja00012a001)
  • 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: 10.1006/jmrb.1994.1127)
  • Sun, H., d'Auvergne, E. J., Reinscheid, U. M., Dias, L. C., Andrade, C. K. Z., Rocha, R. O., and Griesinger, C. (2011). Bijvoet in solution reveals unexpected stereoselectivity in a michael addition. Chem. Eur. J., 17(6), 1811-1817. (DOI: 10.1002/chem.201002520)
  • 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: 10.1021/ja011300z)
  • 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: 10.1080/0026897021000054826)
  • Trott, O. and Palmer, 3rd, A. G. (2002). R1rho relaxation outside of the fast-exchange limit. J. Magn. Reson., 154(1), 157-160. (DOI: 10.1006/jmre.2001.2466)
  • 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: 10.1007/bf00410326)
  • Vallurupalli, P., Hansen, D. F., and Kay, L. E. (2008). Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Proc. Natl. Acad. Sci. USA, 105(33), 11766-11771. (DOI: 10.1073/pnas.0804221105)
  • Vallurupalli, P., Hansen, D. F., Stollar, E., Meirovitch, E. and Kay, L. E. (2007). Measurement of bond vector orientations in invisible excited states of proteins Proc. Natl. Acad. Sci. USA, 104(47), 18473-18477. (DOI: 10.1073/pnas.0708296104)
Retrieved from "http://wiki.nmr-relax.com/wiki/index.php?title=Citations&oldid=7816"