Results from this analysis were broadly consistent with the structural insights inferred using both CD spectra and NMR techniques, with N-Myc73-94 showing two well defined regions in its minimum energy structure: a helical segment spanning the N-terminusresidues 73-86 and a small transient turn regionresidues 88-94that seems to wrap around the Aurora-A αG-helix (Fig. , Fig. ). MD simulations for N-Myc73-94-N85C/G89C-mal revealed a similar and consistent energy minimum Aurora-A bound structure to that observed for the linear peptide, indicating that both peptides could access similar conformations in their Aurora-A bound states (Fig. and Fig. ). We also observed that the maleimide group sits orientated directly towards Aurora-A in proximity to Gln335 AurA , which seems to be conformationally trapped between the maleimide and residues Trp88 N-Myc and Glu84 N-Myc in N-Myc. Analyses of the time averaged structure of both peptides bound to Aurora-A (Fig. ) revealed that for N-Myc73-94 fraying of the helix occurs towards the C-terminus, whilst in comparison the average structure observed for constrained N-Myc73-94-N85C/G89C-mal remains closer to the energy minimum state, with the maleimide constraint potentially interacting via a -amide interaction with Gln335 AurA and preventing the C-terminus from unfolding and undocking from the protein surface. In addition, results from these models also suggest that such an arrangement, where the C-terminus is kept in proximity to Aurora-A due to the maleimide constraint, enables a transient/dynamic close electrostatic interaction between Glu94 N-Myc and Arg343 AurA , which does not take place in the WT peptide due to helix unwinding.