A research of intrinsically disordered proteins attract an increasing
attention because of their unclear role in biological processes and
diseases. The description of internal dynamics of intrinsically
disordered proteins is highly demanded as the attempt for a structural
determination is not relevant. A solution-NMR appears as the optimal
experimental technique for study of such proteins, because the possible
insight into the motion of molecules is one of major benefits of NMR.
Molecular motions at various timescales are usually studied by analyzing
experimental relaxation rates. The investigation of motions within the
unstructured, highly flexible parts of proteins is a challenging task,
because the assumptions required by a standard approaches are not
fulfilled.

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