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Added the Orekhov 1999 reference.
In summary:
* a) Find an initial diffusion tensor estimate (you can do this in relax by only using model m0). This requires all non-mobile residues and side chain spins to be excluded, and this can be problematic. See the [d'Auvergne and Gooley, 2008b] paper for an example of the catastrophic failure that this initial estimate can result in. Or the bacteriorhodopsin fragment of Korzhnev [Orekhov et al., 1999 (http://dx.doi.org/10.1023/a:1008356809071) ] where this complete failure was earlier demonstrated.
* b) Optimise all of the model-free models from m0 to m9. This requires high precision optimisation, for a comparison of all the softwares see the d'Auvergne and Gooley, 2008a model-free optimisation paper at http://dx.doi.org/10.1007/s10858-007-9214-2. Only relax and Dasha implement the full range of model-free models, though the models m6, m7, and m8 cannot be used if only single field strength data is used (m6 is the original 2-time scale motion model of Clore et al., 1990).
* [*d'Auvergne and Gooley, 2008b] 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'''(2), 121-133. (DOI: [http://dx.doi.org/10.1007/s10858-007-9213-3 10.1007/s10858-007-9213-3]).
* [*Orekhov et al., 1999] 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'''(4), 345–356. (DOI: [http://dx.doi.org/10.1023/a:1008356809071 10.1023/a:1008356809071]).
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