When compared, both peptides showed a similar trend in the relative magnitude of Cα secondary shifts at each residue (Fig. , Table ). The most notable divergence between the peptides is observed in the constrained N-Myc region corresponding to residues 85-89, where relatively high Cα secondary shifts were observed for Glu86 N-Myc /Leu87 N-Myc . This indicates the introduction of the chemical constraint may exert a helix stabilizing effect in a region where the WT peptide shows low helical propensity (i.e., Δẟ ~ ẟRC). Both maleimide derivatized residues, Cys85 N-Myc and Cys85 N-Myc , exhibited two out-of-trend negative ΔẟCα values, suggesting that their secondary chemical shifts are either highly affected by the presence of the constraint, or misrepresented due to the lack of an appropriate ẟRC reference for the modified amino-acid. H secondary shifts were also calculated for both peptides (Fig.