To resolve these questions, we have analysed a substantially larger dataset (5 x 1.5 ms for each system of bis-phosphorylated and unphosphorylated state in the wildtype and the cTnC G159D mutant) in a larger box (140 Å cube). We have investigated the effects of phosphorylation and mutation on the dynamics. We observed that the principal motion within troponin was a hinge motion between the NcTnC domain and the "ITC domain"; we identified significant phosphorylation-and mutation-dependent changes in the inter-atom interactions between the disordered segments of troponin and the troponin core using the Arpeggio routine .