Changes

* <section begin=Baldwin14Bain11/>Baldwin {{citation| authors = Bain, A. D., Anand, C. A. (2014), and Nie, Z. An exact | title = Exact solution for R2,eff in of the CPMG experiments in pulse sequence with phase variation down the case of two site chemical exchange. ''echo train: Application to R2 measurements| journal = J. Magn. Reson.'', '''244''', 114-124. (DOI: [http://dx.| volume = 209| issue = 2| page_start = 183| page_end = 194| year = 2011| doi.org/10.1016/j.jmr.2014.02.023 = 10.1016/j.jmr.20142011.0201.023])009}}<section end=Baldwin14Bain11/>

* <section begin=Bieri11Baldwin14/>Bieri, M{{citation| authors = Baldwin A., d'Auvergne, EJ.| title = An exact solution for R2, and Gooley, P. (2011). relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation eff in CPMG experiments in the case of ps-ns and μs motion of proteinstwo site chemical exchange. ''| journal = J. BiomolMagn. NMR'', '''50''', 147-155Reson.| volume = 244| page_start = 114| page_end = 124| year = 2014| doi = 10. (DOI: [http:1016//dxj.doijmr.org/102014.1007/s10858-011-9509-1 1002.1007/s10858-011-9509-1])023}}<section end=Bieri11Baldwin14/>

* <section begin=CarverRichards72Bieri11/>Carver{{citation| authors = Bieri, JM. P, d'Auvergne, E. , and RichardsGooley, RP. E. (1972). General 2-site solution | title = relaxGUI: a new software for chemical exchange produced dependence fast and simple NMR relaxation data analysis and calculation of T2 upon Carrps-Purcell pulse separationns and μs motion of proteins. ''| journal = J. Magn. Reson.'', '''6'''(1), 89-105. (DOI [http://dxBiomol.NMR| volume = 50| page_start = 147| page_end = 155| year = 2011| doi.org/ = 10.10161007/0022s10858-2364(72)90090-X 10.1016/0022011-2364(72)900909509-X])1}}<section end=CarverRichards72Bieri11/>

* <section begin=Clore90BieriGooley11/>Clore{{citation| authors = Bieri, G. M., Szabo, A., Bax, A., Kay, L. E., Driscolland Gooley, P. C., and Gronenborn, A. M. (1990). Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-| title = Automated NMR relaxation of proteinsdispersion data analysis using NESSY. ''J. Am. Chem. Soc.'', '''112'''(| journal = BMC Bioinformatics| volume = 12), 4989-4991. (DOI [http://dx.| page_start = 1| page_end = 10| year = 2011| doi.org/ = 10.10211186/ja00168a070 10.1021/ja00168a070])1471-2105-12-421}}<section end=Clore90BieriGooley11/>

* <section begin=dAuvergneGooley03CarverRichards72/>d'Auvergne{{citation| authors = Carver, EJ. JP. and GooleyRichards, P. R. (2003)E. The use | title = General 2-site solution for chemical exchange produced dependence of model selection in the modelT2 upon Carr-free analysis of protein dynamicsPurcell pulse separation. ''| journal = J. BiomolMagn. Reson. NMR'', '''25'''(| volume = 6| issue = 1), 25-39. (DOI [http://dx.| page_start = 89| page_end = 105| year = 1972| doi.org/ = 10.10231016/a:1021902006114 10.1023/a:1021902006114]0022-2364(72)90090-X}}<section end=dAuvergneGooley03CarverRichards72/>

* <section begin=dAuvergneGooley06Clore90/>d'Auvergne{{citation| authors = Clore, G. M., Szabo, A., Bax, A., Kay, L. E. J, Driscoll, P. C. , and GooleyGronenborn, PA. RM. (2006). Model| title = Deviations from the simple 2-free model elimination: A new step in the parameter model-free dynamic analysis approach to the interpretation of NMR N-15 nuclear magnetic-relaxation dataof proteins. ''| journal = J. BiomolAm. NMR'', '''35'''(2), 117-135Chem. (DOI [http://dxSoc.| volume = 112| issue = 12| page_start = 4989| page_end = 4991| year = 1990| doi.org/10.1007/s10858-006-9007-z = 10.10071021/s10858-006-9007-z])ja00168a070}}<section end=dAuvergneGooley06Clore90/>

* <section begin=dAuvergneGooley07dAuvergne06/>{{citation_thesis| author = d'Auvergne, E. J. and Gooley, P. R. (2007). Set theory formulation | title = Protein dynamics: a study of the model-free problem analysis of NMR relaxation data.| type = PhD| department = Biochemistry and the diffusion seeded modelMolecular Biology| university = University of Melbourne| year = 2006| link = https://minerva-free paradigm. ''Molaccess. BioSystunimelb.'', '''3'''(7), 483–494edu. (DOI: [httpau/handle/11343/39174| pdf = https://dxminerva-access.unimelb.doiedu.orgau/bitstream/handle/11343/10.103939174/b702202f 1067077_00002799_01_thesis.1039/b702202f])pdf?sequence=1}}<section end=dAuvergneGooley07dAuvergne06/>

* <section begin=dAuvergneGooley08adAuvergneGooley03/>{{citation| authors = d'Auvergne, E. J. and Gooley, P. R. (2008a). Optimisation | title = The use of NMR dynamic models I. Minimisation algorithms and their performance within model selection in the model-free and Brownian rotational diffusion spacesanalysis of protein dynamics. ''| journal = J. Biomol. NMR'', '''40'''(2), 107-119. (DOI: [http://dx.| volume = 25| issue = 1| page_start = 25| page_end = 39| year = 2003| doi.org/ = 10.10071023/s10858-007-9214-2 10.1007/s10858-007-9214-2])a:1021902006114}}<section end=dAuvergneGooley08adAuvergneGooley03/>

* <section begin=dAuvergneGooley08bdAuvergneGooley06/>{{citation| authors = d'Auvergne, E. J. and Gooley, P. R. (2008b). Optimisation of NMR dynamic models II. | title = Model-free model elimination: A new methodology for the dual optimisation of step in the model-free parameters and the Brownian rotational diffusion tensordynamic analysis of NMR relaxation data. ''| journal = J. Biomol. NMR'', '''40'''(| volume = 35| issue = 2), 121-133. (DOI: [http://dx.| page_start = 117| page_end = 135| year = 2006| doi.org/10.1007/s10858-007-9213-3 = 10.1007/s10858-007006-92139007-3])z}}<section end=dAuvergneGooley08bdAuvergneGooley06/>

* <section begin=dAuvergneGooley08cdAuvergneGooley07/>{{citation| authors = d'Auvergne, E. J. and Gooley, P. R. (2008c). Optimisation | title = Set theory formulation of NMR dynamic models. ''J. Biomol. NMR'', '''40'''(2), 107the model-133. (DOI: [http://dx.doi.org/10.1007/s10858-007-9214free problem and the diffusion seeded model-2 10free paradigm.1007/s10858-007-9214-2], [http://dx| journal = Mol.doiBioSyst.org/10.1007/s10858-007-9213-| volume = 3 | issue = 7| page_start = 483| page_end = 494| year = 2007| doi = 10.10071039/s10858-007-9213-3])b702202f}}<section end=dAuvergneGooley08cdAuvergneGooley07/>

* <section begin=Davis94dAuvergneGooley08a/>Davis{{citation| authors = d'Auvergne, DE. GJ.and Gooley, Perlman, M. EP., and London, R. E| title = Optimisation of NMR dynamic models I. (1994). Direct measurements of Minimisation algorithms and their performance within the dissociation-rate constant for inhibitormodel-enzyme complexes via the T1rho free and T2 (CPMG) methodsBrownian rotational diffusion spaces. ''| journal = J. Magn. Reson.'', '''104'''(3), 266-275. (DOI [http://dxBiomol.NMR| volume = 40| issue = 2| page_start = 107| page_end = 119| year = 2008| doi.org/ = 10.10061007/jmrb.1994.1084 10.1006/jmrb.1994.1084])s10858-007-9214-2}}<section end=Davis94dAuvergneGooley08a/>

* <section begin=Farrow94dAuvergneGooley08b/>Farrow, N. A.{{citation| authors = d'Auvergne, Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., Kayand Gooley, LP. ER. (1994)| title = Optimisation of NMR dynamic models II. Backbone dynamics A new methodology for the dual optimisation of a the model-free parameters and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxationthe Brownian rotational diffusion tensor. ''Biochemistry'', '''33'''(19), 5984-6003| journal = J. (DOI: [http://dxBiomol.NMR| volume = 40| issue = 2| page_start = 121| page_end = 133| year = 2008| doi.org/ = 10.10211007/bi00185a040 10.1021/bi00185a040])s10858-007-9213-3}}<section end=Farrow94dAuvergneGooley08b/>

* <section begin=Fushman98dAuvergneGooley08c/>Fushman{{citation| authors = d'Auvergne, DE., Tjandra, NJ., and CowburnGooley, DP. (1998)R. Direct measurement | title = Optimisation of ¹⁵N chemical shift anisotropy in solutionNMR dynamic models. ''| journal = J. Am. Chem. Soc.'', '''120'''(42), 10947-10952. (DOI: [http://dxBiomol.NMR| volume = 40| issue = 2| page_start = 107| page_end = 133| year = 2008| doi.org/ = 10.10211007/ja981686m s10858-007-9214-2| doi2 = 10.10211007/ja981686m])s10858-007-9213-3}}<section end=Fushman98dAuvergneGooley08c/>

* <section begin=Korzhnev04aDavis94/>Korzhnev{{citation| authors = Davis, D. MG., KloiberPerlman, KM., Kanelis, V., Tugarinov, VE., and KayLondon, LR. E. (2004a). Probing slow dynamics in high molecular weight proteins by methyl| title = Direct measurements of the dissociation-TROSY NMR spectroscopy: application to a 723rate constant for inhibitor-residue enzymecomplexes via the T1rho and T2 (CPMG) methods. ''| journal = J. AmMagn. Chem. Soc.'', '''126'''(12), 3964-3973. (DOI: [http://dxReson.| volume = 104| issue = 3| page_start = 266| page_end = 275| year = 1994| doi = 10.org1006/10jmrb.1021/ja039587i 101994.1021/ja039587i])1084}}<section end=Korzhnev04aDavis94/>

* <section begin=Korzhnev04bErdelyi11/>Korzhnev{{citation| authors = Erdélyi, D. M., Kloiberd'Auvergne, KE., and KayNavarro-Vázquez, LA. E, Leonov, A. (2004b), and Griesinger, C. Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins| title = Dynamics of the glycosidic bond: theory and application. ''J. Amconformational space of lactose. | journal = Chem. SocEur.'', '''126'''(23), 7320-7329. (DOI: [http://dxJ.| volume = 17| issue = 34| page_start = 9368| page_end = 9376| year = 2011| doi.org/ = 10.10211002/ja049968b 10chem.1021/ja049968b])201100854}}<section end=Korzhnev04bErdelyi11/>

* <section begin=Korzhnev05Evenäs01/>Korzhnev{{citation| authors = Evenäs, D. M., Neudecker, PJ., MittermaierMalmendal, A., Orekhov, V. Y., and KayAkke, LM. E. (2005). Multiple-site exchange in proteins studied with a suite | title = Dynamics of six NMR relaxation dispersion experiments: an application to the folding of transition between open and closed conformations in a Fyn SH3 calmodulin C-terminal domain mutant. ''J. Am. Chem. Soc.'', '''127'''(44), 15602-15611. (DOI: [http://dx.| journal = Structure| volume = 9| issue = 3| page_start = 185| page_end = 195| year = 2001| doi.org/ = 10.10211016/ja054550e 10.1021/ja054550e]S0969-2126(01)00575-5}}<section end=Korzhnev05Evenäs01/>

* <section begin=IshimaTorchia99Farrow94/>Ishima{{citation| authors = Farrow, N. A., Muhandiram, R. and Torchia, DSinger, A. U., Pascal, S. M. A, Kay, C. (2005)M. Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters, Gish, G. ''J, Shoelson, S. BiomolE. NMR'', '''32'''(1)Pawson, 41T., Forman-54Kay, J. (DOI [http://dxD.doi, Kay, L.org/10E.1007/s10858| title = Backbone dynamics of a free and phosphopeptide-005-3593-z 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 = 10.10071021/s10858-005-3593-z])bi00185a040}}<section end=IshimaTorchia99Farrow94/>

* <section begin=LuzMeiboom63Fushman98/>Luz{{citation| authors = Fushman, ZD. , Tjandra, N., and MeiboomCowburn, SD. (1963). Nuclear magnetic resonance study | title = Direct measurement of protolysis of trimethylammonium ion ¹⁵N chemical shift anisotropy in aqueous solution - order of reaction with respect to solvent. ''| journal = J. Am. Chem. Phys.'', '''39'''(2), 366-370. (DOI [http://dxSoc.| volume = 120| issue = 42| page_start = 10947| page_end = 10952| year = 1998| doi.org/10.1063/1.1734254 = 10.10631021/1.1734254])ja981686m}}<section end=LuzMeiboom63Fushman98/>

* <section begin=Meiboom61Fushman99/>Meiboom{{citation| authors = Fushman, D., Tjandra, SN. (1961), and Cowburn, D. Nuclear magnetic resonance study | title = An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of proton transfer in watervariable 15N chemical shift anisotropy and chemical exchange contributions. ''| journal = J. Am. Chem. Phys.'', '''34'''(2), 375-388. (DOI [http://dxSoc.| volume = 121| issue = 37| page_start = 8577| page_end = 8582| year = 1999| doi.org/ = 10.10631021/1.1700960 10.1063/1.1700960]).ja9904991}}<section end=Meiboom61Fushman99/>

* <section begin=MiloushevPalmer05IshimaTorchia99/>Miloushev{{citation| authors = Ishima, V. ZR. and Palmer, 3rdTorchia, D. A. G. (2005). R(1rho) relaxation for two-site | title = Estimating the time scale of chemical exchange: general approximations and some exact solutionsof proteins from measurements of transverse relaxation rates in solution. ''| journal = J. Magn. Reson.'', '''177'''(2), 221-227. (DOI [http://dxBiomol.NMR| volume = 14| issue = 4| page_start = 369| page_end = 372| year = 1999| doi.org/ = 10.10161023/j.jmr.2005.07.023 10.1016/j.jmr.2005.07.023])A:1008324025406}}<section end=MiloushevPalmer05IshimaTorchia99/>

* <section begin=MorinGagné09IshimaTorchia05/>Morin{{citation| authors = Ishima, SR. and GagnéTorchia, SD. (2009)A. Simple tests for the validation of multiple field spin | title = Error estimation and global fitting in transverse-relaxation datadispersion experiments to determine chemical-exchange parameters. ''| journal = J. Biomol. NMR'', '''45''', 361-372. (DOI: [http://dx.| volume = 32| issue = 1| page_start = 41| page_end = 54| year = 2005| doi.org/10.1007/s10858-009-9381-4 = 10.1007/s10858-009005-93813593-4])z}}<section end=MorinGagné09IshimaTorchia99/>

* <section begin=Morin14KempfLoria04/>Morin{{citation| authors = Kempf, S., Linnet, T. E., Lescanne, M., Schanda, PJ., Thompson, G. S., Tollinger, M., Teilum, K., Gagné, S., Marion, D., Griesinger, C., Blackledge, M., and d'AuvergneLoria, E. J. (2014)P. relax: the analysis | title = Measurement of biomolecular kinetics and thermodynamics using NMR relaxation dispersion dataintermediate exchange phenomena. ''Bioinformatics'', '''30'''(15), 2219-2220| journal = Methods Mol. (DOI [http://dxBiol.| volume = 278| page_start = 185| page_end = 231| year = 2004| doi.org/ = 10.10931385/bioinformatics/btu166 10.1093/bioinformatics/btu166])1-59259-809-9:185}}<section end=Morin14KempfLoria04/>

* <section begin=Orekhov99Korzhnev04a/>Orekhov{{citation| authors = Korzhnev, VD. YM., KorzhnevKloiber, D. MK., DiercksKanelis, TV., KesslerTugarinov, HV., and ArsenievKay, AL. SE. (1999). H-1-N| title = Probing slow dynamics in high molecular weight proteins by methyl-15 TROSY NMR dynamic study of an isolated alphaspectroscopy: application to a 723-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitionsresidue enzyme. ''| journal = J. BiomolAm. NMR'', '''14'''(4), 345-356Chem. (DOI: [http://dxSoc.| volume = 126| issue = 12| page_start = 3964| page_end = 3973| year = 2004| doi.org/10.1023/a:1008356809071 = 10.10231021/a:1008356809071])ja039587i}}<section end=Orekhov99Korzhnev04a/>

* <section begin=Palmer91Korzhnev04b/>Palmer{{citation| authors = Korzhnev, 3rd, AD. GM., RanceKloiber, MK., and WrightKay, PL. E. (1991). Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon| title = Multiple-13 heteronuclear quantum relaxation dispersion NMR spectroscopyprobing millisecond time-scale dynamics in proteins: theory and application. ''| journal = J. Am. Chem. Soc.'', '''113'''(12), 4371-4380. (DOI: [http://dx.| volume = 126| issue = 23| page_start = 7320| page_end = 7329| year = 2004| doi.org/10.1021/ja00012a001 = 10.1021/ja00012a001])ja049968b}}<section end=Palmer91Korzhnev04b/>

* <section begin=Schurr94Korzhnev05a/>Schurr{{citation| authors = Korzhnev, JD. M., BabcockNeudecker, HP. P, Mittermaier, A., Orekhov, V. Y., and FujimotoKay, BL. SE. (1994). A test | title = Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the model-free formulas. Effects folding of anisotropic rotational diffusion and dimerizationa Fyn SH3 domain mutant. ''| journal = J. MagnAm. ResonChem. B'', '''105'''(3), 211-224. (DOI: [http://dxSoc.| volume = 127| issue = 44| page_start = 15602| page_end = 15611| year = 2005| doi.org/10.1006/jmrb.1994.1127 = 10.10061021/jmrb.1994.1127])ja054550e}}<section end=Schurr94Korzhnev05a/>

* <section begin=Tollinger01Korzhnev05b/>Tollinger{{citation| authors = Korzhnev, D. M., Skrynnikov, N. R., Mulder, F. A. A., Forman-KayOrekhov, JV. DY., and Kay, L. E. | title = Off-resonance R(20011rho). Slow NMR studies of exchange dynamics in folded and unfolded states of proteins with low spin-lock fields: an sh3 application to a Fyn SH3 domain. ''| journal = J. Am. Chem. Soc.'', '''123'''(46), 11341-11352. (DOI [http://dx.| volume = 127| issue = 2| page_start = 713| page_end = 721| year = 2005| doi.org/10.1021/ja011300z = 10.1021/ja011300z])ja0446855}}<section end=Tollinger01Korzhnev05b/>

* <section begin=TrottPalmer02LipariSzabo82a/>Trott{{citation| authors = Lipari, OG. and Palmer, 3rdSzabo, A. G| title = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules I. (2002). R1rho relaxation outside Theory and range of the fast-exchange limitvalidity. ''| journal = J. MagnAm. ResonChem.'', '''154'''(1), 157-160. (DOI [http://dxSoc.| volume = 104| issue = 17| page_start = 4546| page_end = 4559| year = 1982| doi.org/ = 10.10061021/jmre.2001.2466 10.1006/jmre.2001.2466])ja00381a009}}<section end=TrottPalmer02LipariSzabo82a/>

* <section begin=Trott03LipariSzabo82b/>Trott, O.{{citation| authors = Lipari, Abergel, DG., and PalmerSzabo, A. (2003). An average| title = Model-magnetization analysis free approach to the interpretation of Rnuclear magnetic-1 rho resonance relaxation outside in macromolecules II. Analysis of the fast exchangeexperimental results. ''Mol| journal = J. PhysAm.'', '''101'''(6), 753-763Chem. (DOI [http://dxSoc.| volume = 104| issue = 17| page_start = 4559| page_end = 4570| year = 1982| doi.org/10.1080/0026897021000054826 = 10.10801021/0026897021000054826])ja00381a010}}<section end=Trott03LipariSzabo82b/>

* <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.| volume = 39| issue = 2| page_start = 366| page_end = 370| year = 1963| 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| 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| authors = Meiboom, S.| title = Nuclear magnetic resonance study of proton transfer in water.| journal = J. Chem. Phys.| volume = 34| issue = 2| 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.| volume = 177| issue = 2| 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| volume = 45| 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| volume = 30| issue = 15| page_start = 2219| page_end = 2220| year = 2014| doi = 10.1093/bioinformatics/btu166}}<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| 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| volume = 14| issue = 4| page_start = 345| page_end = 356| year = 1999| doi = 10.1023/a:1008356809071}}<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| 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.| volume = 113| issue = 12| 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| volume = 105| issue = 3| page_start = 211| page_end = 224| year = 1994| doi = 10.1006/jmrb.1994.1127}}<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| 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.| volume = 123| issue = 46| 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.| volume = 101| issue = 6| 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.| volume = 154| issue = 1| 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. (1996). | title = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic. ''| journal = J. Biomol. NMR'', '''| volume = 8'''(| issue = 3), | page_start = 273-| page_end = 284| year = 1996| doi = 10. (DOI: [http:1007/bf00410326}}<section end=Tjandra95/> * <section begin=Vallurupalli08/dx>{{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.org1073/10pnas.10070804221105}}<section end=Vallurupalli08/> * <section begin=Vallurupalli07/bf00410326 >{{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 = 10.10071073/bf00410326])pnas.0708296104}}<section end=Tjandra95Vallurupalli07/> [[Category:Documentation]]