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Nuclear magnetic resonance (NMR) is sensitive to dynamics on a wide range ofcorrelation times. Recently, we have shown that analysis of relaxation ratesvia fitting to a correlation function with a small number of exponential termscould yield a biased characterization of molecular motion in solid-state NMR,due to limited sensitivity of experimental data to certain ranges ofcorrelation times. We introduced an alternative approach based on 'detectors'in solid-state NMR, for which detector responses characterize motion for arange of correlation times, and reduce potential bias resulting from the use ofsimple models for the motional correlation functions. Here, we show thatsimilar bias can occur in the analysis of solution-state NMR relaxation data.We have thus adapted the detector approach to solution-state NMR, specificallyseparating overall tumbling motion from internal motions and accounting forcontributions of chemical exchange to transverse relaxation. We demonstratethat internal protein motions can be described with detectors when the overallmotion and the internal motions are statistically independent. We illustratethe detector analysis on ubiquitin with typical relaxation data sets recordedat a single or at multiple high magnetic fields, and compare with results ofmodel-free analysis. We also compare our methodology to LeMaster's method ofdynamics analysis.

Reducing bias in the analysis of solution-state NMR data with dynamics detectors