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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
| authors = Baldwin A. J.| title = An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange.| journal = J. Magn. Reson.| volume = 244
| page_start = 114
| page_end = 124
| year = 2014
| doi = 10.1016/j.jmr.2014.02.023
}}<section end=Baldwin14/>
* <section begin=Bieri11/>{{citation| authors = Bieri, M., d'Auvergne, E., and Gooley, P. (2011). | 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| volume = 50| page_start = 147| page_end = 155| year = 2011| 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| 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.| volume = 6| issue = 1| 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.| volume = 112| issue = 12| page_start = 4989| page_end = 4991| year = 1990| doi = 10.1021/ja00168a070}}<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| 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| volume = 25| issue = 1| 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| volume = 35| issue = 2| 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.| volume = 3| issue = 7| 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| volume = 40| issue = 2| 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| volume = 40| issue = 2| page_start = 121| page_end = 133| year = 2008| doi = 10.1007/s10858-007-9213-3}}<section end=dAuvergneGooley08b/> * <section begin=dAuvergneGooley08c/>{{citation| authors = d'50''Auvergne, E. J. and Gooley, P. R.| title = Optimisation of NMR dynamic models.| journal = J. Biomol. NMR| volume = 40| issue = 2| page_start = 107| page_end = 133| year = 2008| doi = 10.1007/s10858-007-9214-2| doi2 = 10.1007/s10858-007-9213-3}}<section end=dAuvergneGooley08c/> * <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.| volume = 104| issue = 3| page_start = 266| page_end = 275| year = 1994| doi = 10.1006/jmrb.1994.1084}}<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, 147M.| title = Dynamics of the transition between open and closed conformations in a calmodulin C-155terminal domain mutant.| journal = Structure| volume = 9| issue = 3| page_start = 185| page_end = 195| year = 2001| doi = 10. 1016/S0969-2126(DOI: [http:01)00575-5}}<section end=Evenäs01/> * <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| volume = 33| issue = 19| page_start = 5984| page_end = 6003| year = 1994| doi = 10.1021/bi00185a040}}<section end=Farrow94/> * <section begin=Fushman98/dx>{{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.| volume = 120| issue = 42| page_start = 10947| page_end = 10952| year = 1998| doi = 10.org1021/ja981686m}}<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 = 10.10071021/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/s10858>{{citation| authors = Ishima, R. and Torchia, D. A.| title = Error estimation and global fitting in transverse-011-9509relaxation 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/s10858-011005-95093593-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=Bieri11KempfLoria04/>
* <section begin=CarverRichards72Korzhnev04a/>Carver{{citation| authors = Korzhnev, D. M., Kloiber, K., JKanelis, V. P, Tugarinov, V. , and RichardsKay, RL. E. (1972). General 2| title = Probing slow dynamics in high molecular weight proteins by methyl-site solution for chemical exchange produced dependence of T2 upon CarrTROSY NMR spectroscopy: application to a 723-Purcell pulse separationresidue enzyme. ''| journal = J. MagnAm. ResonChem.'', '''6'''(1), 89-105. (DOI: [http://dxSoc.| volume = 126| issue = 12| page_start = 3964| page_end = 3973| year = 2004| doi.org/ = 10.10161021/0022-2364(72)90090-X 10.1016/0022-2364(72)90090-X])ja039587i}}<section end=CarverRichards72Korzhnev04a/>
* <section begin=Clore90Korzhnev04b/>Clore{{citation| authors = Korzhnev, GD. M., SzaboKloiber, A., Bax, AK., and Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. (1990). Deviations from the simple 2| title = Multiple-parameter modelquantum relaxation dispersion NMR spectroscopy probing millisecond time-free approach to the interpretation of N-15 nuclear magnetic-relaxation of scale dynamics in proteins: theory and application. ''| journal = J. Am. Chem. Soc.'', '''112'''(12), 4989-4991. (DOI: [http://dx.| volume = 126| issue = 23| page_start = 7320| page_end = 7329| year = 2004| doi.org/10.1021/ja00168a070 = 10.1021/ja00168a070])ja049968b}}<section end=Clore90Korzhnev04b/>
* <section begin=dAuvergneGooley03Korzhnev05a/>d'Auvergne{{citation| authors = Korzhnev, ED. JM. and Gooley, Neudecker, P. R, Mittermaier, A. (2003), Orekhov, V. Y. The use , and Kay, L. E.| title = Multiple-site exchange in proteins studied with a suite of model selection in six NMR relaxation dispersion experiments: an application to the model-free analysis folding of protein dynamicsa Fyn SH3 domain mutant. ''| journal = J. BiomolAm. NMR'', '''25'''(1), 25-39Chem. (DOI: [http://dxSoc.| volume = 127| issue = 44| page_start = 15602| page_end = 15611| year = 2005| doi.org/10.1023/a:1021902006114 = 10.10231021/a:1021902006114])ja054550e}}<section end=dAuvergneGooley03Korzhnev05a/>
* <section begin=dAuvergneGooley06Korzhnev05b/>d'Auvergne{{citation| authors = Korzhnev, D. M., EOrekhov, V. JY. , and GooleyKay, PL. E. | title = Off-resonance R. (20061rho). ModelNMR studies of exchange dynamics in proteins with low spin-free model eliminationlock fields: A new step in the model-free dynamic analysis of NMR relaxation dataan application to a Fyn SH3 domain. ''| journal = J. BiomolAm. NMR'', '''35'''(2), 117-135Chem. (DOI: [http://dxSoc.| volume = 127| issue = 2| page_start = 713| page_end = 721| year = 2005| doi.org/ = 10.10071021/s10858-006-9007-z 10.1007/s10858-006-9007-z])ja0446855}}<section end=dAuvergneGooley06Korzhnev05b/>
* <section begin=dAuvergneGooley07LipariSzabo82a/>d'Auvergne{{citation| authors = Lipari, E. JG. and GooleySzabo, PA. R. (2007). Set theory formulation of the model| title = Model-free problem and approach to the diffusion seeded modelinterpretation of nuclear magnetic-free paradigmresonance relaxation in macromolecules I. Theory and range of validity. ''Mol| journal = J. BioSystAm.'', '''3'''(7), 483–494Chem. (DOI: [http://dxSoc.| volume = 104| issue = 17| page_start = 4546| page_end = 4559| year = 1982| doi.org/10.1039/b702202f = 10.10391021/b702202f])ja00381a009}}<section end=dAuvergneGooley07LipariSzabo82a/>
* <section begin=dAuvergneGooley08aLipariSzabo82b/>d'Auvergne{{citation| authors = Lipari, E. JG. and GooleySzabo, PA. R| title = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules II. (2008a). Optimisation Analysis of NMR dynamic models Iexperimental results. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. ''| journal = J. BiomolAm. NMR'', '''40'''(2), 107-119Chem. (DOI: [http://dxSoc.| volume = 104| issue = 17| page_start = 4559| page_end = 4570| year = 1982| doi.org/10.1007/s10858-007-9214-2 = 10.10071021/s10858-007-9214-2])ja00381a010}}<section end=dAuvergneGooley08aLipariSzabo82b/>
* <section begin=dAuvergneGooley08bLuzMeiboom63/>d'Auvergne{{citation| authors = Luz, E. JZ. and GooleyMeiboom, PS. R. (2008b). Optimisation | title = Nuclear magnetic resonance study of NMR dynamic models II. A new methodology for the dual optimisation protolysis of the modeltrimethylammonium ion in aqueous solution -free parameters and the Brownian rotational diffusion tensororder of reaction with respect to solvent. ''| journal = J. BiomolChem. Phys. NMR'', '''40'''(| volume = 39| issue = 2), 121-133. (DOI: [http://dx.| page_start = 366| page_end = 370| year = 1963| doi.org/ = 10.10071063/s10858-007-9213-3 101.1007/s10858-007-9213-3])1734254}}<section end=dAuvergneGooley08bLuzMeiboom63/>
* <section begin=dAuvergneGooley08cMandel95/>d'Auvergne{{citation| authors = Mandel, EA. M. J, Akke, M. , and GooleyPalmer, P3rd, A. RG. (2008c). Optimisation | title = Backbone dynamics of NMR dynamic models. ''J. Biomol. NMR'', Escherichia coli'''40'''(2), 107-133. (DOIribonuclease HI: [http://dxcorrelations with structure and function in an active enzyme.doi| journal = J.org/10Mol.1007/s10858-007-9214-2 10.1007/s10858-007-9214-2], [http://dxBiol.| volume = 246| issue = 1| page_start = 144| page_end = 163| year = 1995| doi = 10.org1006/10jmbi.1007/s10858-007-9213-3 101994.1007/s10858-007-9213-3])0073}}<section end=dAuvergneGooley08cMandel95/>
* <section begin=Davis94Massi05/>Davis{{citation| authors = Massi, D. GF., PerlmanGrey, M. EJ., and LondonPalmer, R3rd, A. EG. (1994). Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods. ''J. Magn. Reson.'', '''104'''(| title = Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments| journal = Protein science| volume = 14| issue = 3), 266-275. (DOI: [http://dx.| page_start = 735| page_end = 742| year = 2005| doi.org/10.1006/jmrb.1994.1084 = 10.10061110/jmrb.1994ps.1084])041139505}}<section end=Davis94Massi05/>
* <section begin=Farrow94Meiboom61/>Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal{{citation| authors = Meiboom, S. M| title = Nuclear magnetic resonance study of proton transfer in water., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, | journal = J. D., Kay, L. EChem. (1994)Phys. Backbone dynamics of a free and phosphopeptide-complexed Src homology | volume = 34| issue = 2 domain studied by 15N NMR relaxation. ''Biochemistry'', '''33'''(19), 5984-6003. (DOI: [http://dx.| page_start = 375| page_end = 388| year = 1961| doi.org/ = 10.10211063/bi00185a040 101.1021/bi00185a040])1700960}}<section end=Farrow94Meiboom61/>
* <section begin=Fushman98MiloushevPalmer05/>Fushman{{citation| authors = Miloushev, DV.Z. and Palmer, Tjandra3rd, NA., and Cowburn, DG. | title = R(19981rho). Direct measurement of <sup>15</sup>N relaxation for two-site chemical shift anisotropy in solutionexchange: general approximations and some exact solutions. ''| journal = J. AmMagn. ChemReson. Soc| volume = 177| issue = 2| page_start = 221| page_end = 227| year = 2005| doi = 10.'', '''120'''(42), 10947-10952. (DOI: [http:1016//dxj.doijmr.org/102005.1021/ja981686m 1007.1021/ja981686m])023}}<section end=Fushman98MiloushevPalmer05/>
* <section begin=Korzhnev04aMorinGagné09/>Korzhnev, D. M.{{citation| authors = Morin, Kloiber, KS., Kanelis, V., Tugarinov, V., and KayGagné, LS. E| title = Simple tests for the validation of multiple field spin relaxation data. (2004). Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. ''| journal = J. Am. Chem. Soc.'', '''126'''(12), 3964-3973. (DOI: [http://dxBiomol.NMR| volume = 45| page_start = 361| page_end = 372| year = 2009| doi.org/ = 10.10211007/ja039587i 10.1021/ja039587i])s10858-009-9381-4}}<section end=Korzhnev04aMorinGagné09/>
* <section begin=Korzhnev04bMorin14/>Korzhnev{{citation| authors = Morin, DS., Linnet, T. E. , Lescanne, M., KloiberSchanda, KP., and KayThompson, LG. ES. (2004), Tollinger, M. Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application, Teilum, K. ''J, Gagné, S. Am, Marion, D. Chem, Griesinger, C. Soc, Blackledge, M.'', and d'''126'''(23)Auvergne, 7320-7329E. J. (DOI| title = relax: [http://dxthe analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data.| journal = Bioinformatics| volume = 30| issue = 15| page_start = 2219| page_end = 2220| year = 2014| doi.org/ = 10.10211093/ja049968b 10.1021bioinformatics/ja049968b])btu166}}<section end=Korzhnev04bMorin14/>
* <section begin=Korzhnev05aMyintIshima09/>Korzhnev, D. M., Neudecker, P., Mittermaier, A.{{citation| authors = Myint, Orekhov, VW. Y., and KayIshima, LR. E. (2005). Multiple-site | title = Chemical exchange effects during refocusing pulses in proteins studied with a suite of six NMR constant-time CPMG relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. ''| journal = J. Am. Chem. Soc.'', '''127'''(44), 15602-15611. (DOI: [http://dxBiomol.NMR| volume = 45| issue = 1| page_start = 207| page_end = 216| year = 2009| doi.org/ = 10.10211007/ja054550e 10.1021/ja054550e])s10858-009-9344-9}}<section end=Korzhnev05aMyintIshima09/>
* <section begin=Korzhnev05bOrekhov95/>Korzhnev, D. M., {{citation| authors = Orekhov, V. Y., and KayNolde, LD. E. (2005), Golovanov, A. Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domainP. ''J, Korzhnev, D. AmM. Chemand Arseniev, A. SocS.'', '''127'''(2), 713-721| title = Processing of heteronuclear NMR relaxation data with the new software DASHA| journal = Appl. Magn. (DOI: [http://dxReson.| volume = 9| issue = 4| page_start = 581| page_end = 588| year = 1995| doi.org/10.1021/ja0446855 = 10.10211007/ja0446855])bf03162365}}<section end=Korzhnev05bOrekhov95/>
* <section begin=IshimaTorchia99Orekhov99/>Ishima{{citation| authors = Orekhov, RV. Y. and Torchia, Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. (2005)S. Error estimation and global fitting in transverse| title = H-1-relaxation dispersion experiments to determine chemicalN-exchange parameters. ''J. Biomol. 15 NMR'', '''32'''dynamic study of an isolated alpha-helical peptide (1-36), 41bacteriorhodopsin reveals the equilibrium helix-54coil transitions.| journal = J. (DOI: [http://dxBiomol.NMR| volume = 14| issue = 4| page_start = 345| page_end = 356| year = 1999| doi.org/ = 10.10071023/s10858-005-3593-z 10.1007/s10858-005-3593-z])a:1008356809071}}<section end=IshimaTorchia99Orekhov99/>
* <section begin=LuzMeiboom63Palmer01/>Luz{{citation| authors = Palmer, 3rd, A. G., Kroenke, ZC. D. , and MeiboomLoria, SJ. (1963)P. | title = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution methods for quantifying microsecond- order of reaction with respect to solvent. ''J. Chem. Phys.'', '''39'''(2), 366-370millisecond motions in biological macromolecules. (DOI: [http://dx| journal = Methods Enzymol.| volume = 339| page_start = 204| page_end = 238| year = 2001| doi.org/ = 10.10631016/S0076-6879(01)39315-1.1734254 10.1063/1.1734254])}}<section end=LuzMeiboom63Palmer01/>
* <section begin=Meiboom61PalmerMassi06/>Meiboom{{citation| authors = Palmer, 3rd, SA. G. (1961)and Massi, F. Nuclear magnetic resonance study | title = Characterization of the dynamics of proton transfer in water. ''Jbiomacromolecules using rotating-frame spin relaxation NMR spectroscopy. | journal = Chem. Phys.'', '''34'''(2), 375-388. (DOI: [http://dxRev.| volume = 106| issue = 5| page_start = 1700| page_end = 1719| year = 2006| doi.org/ = 10.10631021/1.1700960 10.1063/1.1700960]).cr0404287}}<section end=Meiboom61PalmerMassi06/>
* <section begin=MiloushevPalmer05Palmer91/>Miloushev, V. Z. and {{citation| authors = Palmer, 3rd, A. G. (2005), Rance, M. R(1rho) relaxation for two-site chemical exchange: general approximations , and some exact solutionsWright, P. ''JE. Magn. Reson.'', '''177'''(2), 221| title = Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-22713 heteronuclear NMR spectroscopy. (DOI: [http://dx| journal = J.doiAm.org/10Chem.1016/jSoc.jmr.2005.07.023 | volume = 113| issue = 12| page_start = 4371| page_end = 4380| year = 1991| doi = 10.10161021/j.jmr.2005.07.023])ja00012a001}}<section end=MiloushevPalmer05Palmer91/>
* <section begin=MorinGagné09Schurr94/>Morin{{citation| authors = Schurr, J. M., Babcock, SH. P. , and GagnéFujimoto, B. S. (2009)| title = A test of the model-free formulas. Simple tests for the validation Effects of multiple field spin relaxation dataanisotropic rotational diffusion and dimerization. ''| journal = J. Biomol. NMR'', '''45''', 361-372Magn. (DOI: [http://dxReson.B| volume = 105| issue = 3| page_start = 211| page_end = 224| year = 1994| doi = 10.org1006/10jmrb.1007/s10858-009-9381-4 101994.1007/s10858-009-9381-4])1127}}<section end=MorinGagné09Schurr94/>
* <section begin=Morin14Sun11/>Morin{{citation| authors = Sun, SH., Linnetd'Auvergne, TE. EJ., LescanneReinscheid, U. M., SchandaDias, PL., Thompson, G. SC., TollingerAndrade, MC., Teilum, K. Z., GagnéRocha, SR., Marion, DO., and Griesinger, C., Blackledge, M| title = Bijvoet in solution reveals unexpected stereoselectivity in a michael addition.| journal = Chem., and d'Auvergne, EEur. J. (2014). relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. ''Bioinformatics'', '''30'''(15), 2219-2220. (DOI: [http://dx.| volume = 17| issue = 6| page_start = 1811| page_end = 1817| year = 2011| doi.org/ = 10.1093/bioinformatics1002/btu166 10chem.1093/bioinformatics/btu166])201002520}}<section end=Morin14Sun11/>
* <section begin=Orekhov99Tollinger01/>Orekhov{{citation| authors = Tollinger, V. YM., KorzhnevSkrynnikov, DN. MR., DiercksMulder, TF. A. A., KesslerForman-Kay, HJ. D., and ArsenievKay, AL. SE. (1999). H-1-N-15 NMR dynamic study | title = Slow dynamics in folded and unfolded states of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitionssh3 domain. ''| journal = J. BiomolAm. NMR'', '''14'''(4), 345-356Chem. (DOI: [http://dxSoc.| volume = 123| issue = 46| page_start = 11341| page_end = 11352| year = 2001| doi.org/10.1023/a:1008356809071 = 10.10231021/a:1008356809071])ja011300z}}<section end=Orekhov99Tollinger01/>
* <section begin=Palmer91Trott03/>Palmer{{citation| authors = Trott, 3rd, A. GO., RanceAbergel, MD., and WrightPalmer, PA. E. (1991). Intramolecular motions | title = An average-magnetization analysis of a zinc finger DNAR-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy1 rho relaxation outside of the fast exchange. ''J| journal = Mol. Am. Chem. Soc.'', '''113'''(12), 4371-4380. (DOI: [http://dxPhys.| volume = 101| issue = 6| page_start = 753| page_end = 763| year = 2003| doi.org/10.1021/ja00012a001 = 10.10211080/ja00012a001])0026897021000054826}}<section end=Palmer91Trott03/>
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