By edited by Graham A. Webb.
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Extra resources for Annual Reports on NMR Spectroscopy
By utilizing LGCP-based separated-local-field experiments, site-specific order parameters collected from their DCs for microcrystalline U-13C,15N-ubiquitin give rise to data for their backbone and side-chain dynamics . The order parameters thus obtained were compared to solution NMR order parameter: the solid state measurements are sensitive to motions on a broader time scale (low microsecond and faster) than solution NMR measurements (low nanosecond and faster), and the solid state NMR order parameters are generally lower than the corresponding solution values.
B) Typical fits of dispersion data with a global three-state folding model for Ser 41(G48M) of the Fyn SH3 domain. (C) Values of kf and ku for selected residues (labelled with residue number) from fits of dispersions assuming a two-state model at 35 ºC for G48M. (D) Populations (U and I in pink (grey in print version); scale on left-hand side) and exchange rates (UI ¼ kUI +kIU, IF ¼ kIF +kFI in purple (dark grey in print version); scale on right-hand side) as a function of temperature, along with thermodynamic parameters (inset in left corner).
S. P. Loria, Off-resonance TROSY (R1ρ-R1) for quantitation of fast exchange processes in large proteins, J. Am. Chem. Soc. 125 (2003) 12064–12065. I. G. Palmer III, Off-resonance TROSY-selected R1ρ experiment with improved sensitivity for medium- and high-molecular-weight proteins, J. Am. Chem. Soc. 128 (2006) 8110–8111.  J. Dittmer, G. Bodenhausen, Evidence for slow motion in proteins by multiple refocusing of heteronuclear nitrogen/proton multiple quantum coherence in NMR, J. Am. Chem. Soc.
Annual Reports on NMR Spectroscopy by edited by Graham A. Webb.