Citations

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, 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)

• 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, 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, 4989-4991. (DOI: 10.1021/ja00168a070)

• 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, 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, 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, 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, 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, 121-133. (DOI: 10.1007/s10858-007-9213-3)

• d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models. J. Biomol. NMR, 40, 107-133. (DOI: 10.1007/s10858-007-9214-2, 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, 266-275. (DOI: 10.1006/jmrb.1994.1084)

• 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, 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, 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, 10947-10952. (DOI: 10.1021/ja981686m)

• 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, 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, 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, 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, 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, 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, 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, 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, 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, 366-370. (DOI: 10.1063/1.1734254)

• 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, 735-742. (DOI: 10.1110/ps.041139505)

• Meiboom, S. (1961). Nuclear magnetic resonance study of proton transfer in water. J. Chem. Phys., 34, 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, 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, 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, 207-216. (DOI: 10.1007/s10858-009-9344-9)

• 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, 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, 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, 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, 211-224. (DOI: 10.1006/jmrb.1994.1127)

• 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, 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, 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, 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, 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, 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, 18473-18477. (DOI: 10.1073/pnas.0708296104)