Abstract
Structural analyses of proteins by NMR often rely on paramagnetic relaxation enhancement (PRE) data. This is especially true for challenging protein targets, e.g. large, unstable or poorly soluble proteins. To acquire PRE data, protein samples are labeled with a paramagnetic tag, such as MTSL, and the resulting attenuation of peak intensities in the 1HN,15N-HSQC spectra is measured. However, the relationship between the PRE rates and the distances r from paramagnetic center to specific 1HN atoms is subject to considerable uncertainty (mainly due to conformational mobility of the tag).
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