Regular ArticleA Relaxation-Matrix Analysis of Distance-Constraint Ranges for NOEs in Proteins at Long Mixing Times
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The nuclear Overhauser effect from a quantitative perspective
2014, Progress in Nuclear Magnetic Resonance SpectroscopyCitation Excerpt :Although longer mixing times cause larger uncertainties, theoretically, iterative structure calculations and correction for spin diffusion should also converge for long mixing times. Previously, a simple approach to run longer NOESY mixing times and thus extract many more long distances was based on a statistical analysis of the distance-intensity relationship [209]. Simulations of spectra with mixing times up to 400 ms for protonated proteins with 2 and 5 ns tumbling times show that possibly hundreds of additional peaks may be evaluated.
Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle
2002, Journal of Molecular BiologySolution structure, backbone dynamics, and stability of a double mutant single-chain monellin: Structural origin of sweetness
2001, Journal of Biological ChemistryCitation Excerpt :All two-dimensional experiments were performed at 298 K. Pulsed-field gradient techniques were used for all H2O experiments, resulting in good suppression of the solvent signal.15N-1H HSQC (18, 19) spectra were recorded with a uniformly 15N-labeled sample with 2048 complex data points in t 2 and 256 t 1increments. Two-dimensional nuclear Overhauser effect spectroscopy (NOESY) (20, 21) spectra were recorded with mixing times with 100 ms and 150 ms in H2O and D2O solution. Two-dimensional total correlation spectroscopy (TOCSY) (22) spectrum was acquired in H2O solution with a mixing time of 69.668 ms using MLEV17 spin lock pulses.
Investigation of Uncertainties in Relaxation Analysis of 2D NOE Which Arise from Spectral Noise
1997, Journal of Magnetic Resonance