dynamic landscape that needs to be described by a large number of parameters . MD simulations could be used, but they require a careful selection of simulation parameters and a substantial amount of computational resources . Furthermore, direct comparisons of dynamics between different proteins is challenging in many cases because data is often acquired with different magnetic fields which also affects the spin relaxation rates. Our analysis circumvents these challenges and enables rapid interpretation of rotational dynamics of residues directly from experimental R2 values for a wide range of protein and peptide systems. For folded proteins, results from the linear approximation presented in this work are in line with the standard Lipari-Szabo analysis in supplementary figure .