 The MD simulation provided a wealth of information on the interactions between MTSL and protein residues, and on the different motional contributions to the overall dynamics of the MTSL that were validated using a multifrequency electron paramagnetic resonance (EPR) approach. The latter relayed on the frequency dependence of the resolution of the fast and slow motions of the spin probe and was used to distinguish the fast internal motion of the spin label from the slow protein tumbling.
<clarity>  The MD simulation provided a wealth of information on the interactions between MTSL and protein residues, and on the different motional contributions to the overall dynamics of the MTSL that were validated using a multifrequency electron paramagnetic resonance (EPR) approach. The latter relayed on the frequency dependence of the resolution of the fast and slow motions of the spin probe and was used to distinguish the fast internal motion of the spin label from the slow protein tumbling.
 The MD simulation provided a wealth of information on the interactions between MTSL and protein residues, and on the different motional contributions to the overall dynamics of the MTSL that were validated using a multifrequency electron paramagnetic resonance (EPR) measurements, that relying on the frequency dependence of the resolution of the fast and slow motions of the spin probe and was used to distinguish the fast internal motion of the spin label from the slow protein tumbling.