Molecular dynamics simulations supported both the timescale and collective nature of motions of the β-hairpin. This seminal study was followed by investigations by high-resolution relaxometry, combined with traditional high-field NMR, of the internal dynamics of proteins such as ubiquitin. To measure site-specific low-field relaxation rates, a pneumatic shuttling system was developed, enabling rapid transfer of samples between the magnetic center and the chosen position of the stray field. This system facilitated high-resolution measurements of longitudinal relaxation rates at low fields, although with reduced sensitivity compared to high-field experiments (about ten times less sensitivity) due to system design. This setup allowed the measurement of relaxation rates over a wide range of fields (0.5-14.1 T), correcting for systematic deviations of decay rates due to cross-relaxation using an iterative correction approach called ICARUS, which accounts for the effects of cross-relaxation pathways during shuttling. The ICARUS corrections for backbone nitrogen-15 decays varied between 4.5% and 13%, with greater corrections needed at fields below 3 T. The analysis of low-field longitudinal relaxation rates revealed dynamics in the 𝛽 1 -𝛽 2 turn of ubiquitin on the nanosecond timescale, which exhibited nanosecond motions that were not identified with a similar amplitude in earlier studies at a single high magnetic field but highlighted by the analysis of residual dipolar couplings. These motions were best described by an extended model-free analysis, occurring with a timescale of τ 7-9 ~ 2 ns, suggesting a collective motion in this region. Relaxometry dispersion profiles (Figure ) highlight the differences between mobile and rigid residues, with nanosecond motions dominating at lower fields. While the experimental data mostly align with theoretical predictions, some discrepancies in the dispersion profiles, particularly for highly mobile residues like Gly75 and Gly76, suggested limitations in models of spectral density functions.