Changes

* <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.| 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'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, 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| 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/>{{citation| authors = Fushman, D., Tjandra, N., and Cowburn, D.| title = Direct measurement of ¹⁵N chemical shift anisotropy in solution.| journal = J. Am. Chem. Soc.| volume = 120| issue = 42| page_start = 10947| page_end = 10952| year = 1998| doi = 10.1021/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 = 10.1021/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| authors = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E.| title = Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme.| journal = J. Am. Chem. Soc.| volume = 126| issue = 12| page_start = 3964| page_end = 3973| year = 2004| doi = 10.1021/ja039587i}}<section end=Korzhnev04a/> * <section begin=Korzhnev04b/>{{citation| authors = Korzhnev, D. M., Kloiber, K., and Kay, L. E.| title = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application.| journal = J. Am. Chem. Soc.| volume = 126| issue = 23| page_start = 7320| page_end = 7329| year = 2004| doi = 10.1021/ja049968b}}<section end=Korzhnev04b/> * <section begin=Korzhnev05a/>{{citation| authors = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E.| title = Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant.| journal = J. Am. Chem. Soc.| volume = 127| issue = 44| page_start = 15602| page_end = 15611| year = 2005| doi = 10.1021/ja054550e}}<section end=Korzhnev05a/> * <section begin=Korzhnev05b/>{{citation| authors = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E.| title = Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain.| journal = J. Am. Chem. Soc.| volume = 127| issue = 2| page_start = 713| page_end = 721| year = 2005| doi = 10.1021/ja0446855}}<section end=Korzhnev05b/> * <section begin=LipariSzabo82a/>{{citation| authors = Lipari, G. and Szabo, A.| title = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules I. Theory and range of validity.| journal = J. Am. Chem. Soc.| volume = 104| issue = 17| page_start = 4546| page_end = 4559| year = 1982| doi = 10.1021/ja00381a009}}<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| 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. (2014). | 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, '''30''' A. S.| title = H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (151-36)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., 2219and Loria, J. P.| title = Nuclear magnetic resonance methods for quantifying microsecond-to-2220millisecond motions in biological macromolecules.| journal = Methods Enzymol.| volume = 339| page_start = 204| page_end = 238| year = 2001| doi = 10. 1016/S0076-6879(DOI [http: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/dx>{{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.org2466}}<section end=TrottPalmer02/> * <section begin=Tjandra95/>{{citation| authors = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A.| title = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic.| journal = J. Biomol. NMR| volume = 8| issue = 3| page_start = 273| page_end = 284| year = 1996| doi = 10.10931007/bf00410326}}<section end=Tjandra95/bioinformatics> * <section begin=Vallurupalli08/btu166 >{{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 = 10.10931073/pnas.0804221105}}<section end=Vallurupalli08/> * <section begin=Vallurupalli07/bioinformatics>{{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/btu166])pnas.0708296104}}<section end=Morin14Vallurupalli07/> [[Category:Documentation]]