To characterize the amplitude of dynamic processes in molecules, anisotropic parameters can be measured using solid-state NMR. However, the timescales of motion that lead to such a scaling of the anisotropic interactions are not clear. Using numerical simulations in small spin systems, we could show that mostly the magnitude of the anisotropic interaction determines the range of timescales detected by the scaled anisotropic interaction, and experimental parameters play a very minor role.

NMR studies can be of great help in understanding the molecular mechanisms of nucleosome functions. For solid-state NMR, nucleosomes need to be tightly packed together. We show that centrifugation of nucleosomes results in formation of gels with very high packing ratios yet without pronounced order in the packing and without formation of specific or stable inter-nucleosome contacts. This makes the approach suitable also for the study of proteins that bind weakly to the nucleosome.