*4.3. Chemical Shift Deviation*

Sequence-specific assignments for all peptides were completed by using the 2D-NMR spectra (TOCSY and ROESY). The chemical shift deviation (∆δHα) for each residue of the experimental peptide ∆δHα(exp)) and the folded reference peptide (∆δHα(F)) was derived using Equations (1) and (2), respectively [38]. δHα(exp) is the chemical shift for the residue of interest on the experimental peptide, and δHα(U) is the chemical shift for the corresponding residue of interest on the fully unfolded reference peptide. δHα(F) is the chemical shift for the residue of interest on the fully folded reference peptide.

$$
\Delta \delta \mathbf{H} \alpha (\exp) = \delta \mathbf{H} \alpha (\exp) - \delta \mathbf{H} \alpha (\mathbf{U}) \tag{1}
$$

$$
\Delta \delta \mathbf{H} \alpha(\mathbf{F}) = \delta \mathbf{H} \alpha(\mathbf{F}) - \delta \mathbf{H} \alpha(\mathbf{U}) \tag{2}
$$
