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| journal = J. Magn. Reson.
| volume = 209
| number issue = 2
| page_start = 183
| page_end = 194
| doi = 10.1007/s10858-011-9509-1
}}<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
| journal = J. Magn. Reson.
| volume = 6
| number issue = 1
| page_start = 89
| page_end = 105
| journal = J. Am. Chem. Soc.
| volume = 112
| number issue = 12
| page_start = 4989
| page_end = 4991
| journal = J. Biomol. NMR
| volume = 25
| number issue = 1
| page_start = 25
| page_end = 39
| journal = J. Biomol. NMR
| volume = 35
| number issue = 2
| page_start = 117
| page_end = 135
| journal = Mol. BioSyst.
| volume = 3
| number issue = 7
| page_start = 483
| page_end = 494
| journal = J. Biomol. NMR
| volume = 40
| number issue = 2
| page_start = 107
| page_end = 119
| journal = J. Biomol. NMR
| volume = 40
| number issue = 2
| page_start = 121
| page_end = 133
| journal = J. Biomol. NMR
| volume = 40
| number issue = 2
| page_start = 107
| page_end = 133
| journal = J. Magn. Reson.
| volume = 104
| number issue = 3
| page_start = 266
| page_end = 275
* <section begin=Erdelyi11/>{{citation
| authors = ErdelyiErdélyi, M., d'Auvergne, E., Navarro-VazquezVázquez, A., Leonov, A., and Griesinger, C.
| title = Dynamics of the glycosidic bond: conformational space of lactose.
| journal = Chem. Eur. J.
| volume = 17
| number issue = 34
| page_start = 9368
| page_end = 9376
| journal = Structure
| volume = 9
| number issue = 3
| page_start = 185
| page_end = 195
| journal = Biochemistry
| volume = 33
| number issue = 19
| page_start = 5984
| page_end = 6003
| journal = J. Am. Chem. Soc.
| volume = 120
| number issue = 42
| page_start = 10947
| page_end = 10952
| journal = J. Am. Chem. Soc.
| volume = 121
| number issue = 37
| page_start = 8577
| page_end = 8582
| journal = J. Biomol. NMR
| volume = 14
| number issue = 4
| page_start = 369
| page_end = 372
| journal = J. Biomol. NMR
| volume = 32
| number issue = 1
| page_start = 41
| page_end = 54
| journal = J. Am. Chem. Soc.
| volume = 126
| number issue = 12
| page_start = 3964
| page_end = 3973
| journal = J. Am. Chem. Soc.
| volume = 126
| number issue = 23
| page_start = 7320
| page_end = 7329
| journal = J. Am. Chem. Soc.
| volume = 127
| number issue = 44
| page_start = 15602
| page_end = 15611
| journal = J. Am. Chem. Soc.
| volume = 127
| number issue = 2
| page_start = 713
| page_end = 721
| journal = J. Am. Chem. Soc.
| volume = 104
| number issue = 17
| page_start = 4546
| page_end = 4559
| journal = J. Am. Chem. Soc.
| volume = 104
| number issue = 17
| page_start = 4559
| page_end = 4570
| journal = J. Chem. Phys.
| volume = 39
| number issue = 2
| page_start = 366
| page_end = 370
| doi = 10.1063/1.1734254
}}<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
| journal = Protein science
| volume = 14
| number issue = 3
| page_start = 735
| page_end = 742
| journal = J. Chem. Phys.
| volume = 34
| number issue = 2
| page_start = 375
| page_end = 388
| journal = J. Magn. Reson.
| volume = 177
| number issue = 2
| page_start = 221
| page_end = 227
| journal = Bioinformatics
| volume = 30
| number issue = 15
| page_start = 2219
| page_end = 2220
| journal = J. Biomol. NMR
| volume = 45
| number issue = 1
| page_start = 207
| page_end = 216
| 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
| journal = J. Biomol. NMR
| volume = 14
| number issue = 4
| page_start = 345
| page_end = 356
| journal = Chem. Rev.
| volume = 106
| number issue = 5
| page_start = 1700
| page_end = 1719
| journal = J. Am. Chem. Soc.
| volume = 113
| number issue = 12
| page_start = 4371
| page_end = 4380
| journal = J. Magn. Reson. B
| volume = 105
| number issue = 3
| page_start = 211
| page_end = 224
| journal = Chem. Eur. J.
| volume = 17
| number issue = 6
| page_start = 1811
| page_end = 1817
| journal = J. Am. Chem. Soc.
| volume = 123
| number issue = 46
| page_start = 11341
| page_end = 11352
| journal = Mol. Phys.
| volume = 101
| number issue = 6
| page_start = 753
| page_end = 763
| journal = J. Magn. Reson.
| volume = 154
| number issue = 1
| page_start = 157
| page_end = 160
| journal = J. Biomol. NMR
| volume = 8
| number issue = 3
| page_start = 273
| page_end = 284
| journal = Proc. Natl. Acad. Sci. USA
| volume = 105
| number issue = 33
| page_start = 11766
| page_end = 11771
| journal = Proc. Natl. Acad. Sci. USA
| volume = 104
| number issue = 47
| page_start = 18473
| page_end = 18477
| doi = 10.1073/pnas.0708296104
}}<section end=Vallurupalli07/>
[[Category:Documentation]]