In the plot of the corresponding relative energies of the conformers in Fig. , we recognize that the eb-MFCC and db-MFCC cannot reproduce the energy ordering of the conformers correctly, even though they partly follow the correct trend. The relative energies from the eb-MFCC-MBE(2) and db-MFCC-MBE(2) schemes both closely follow the super- Across all three structures, only the db-MFCC-MBE(2) scheme is able to provide consistent relative energies for the different polypeptide conformers. In cases with strong intramolecular interactions, such as those present in the α-helical structures, the inclusion of the density-based correction is essential for an accurate description of these interactions. For the turn and β-strand structures, the intermolecular interactions can largely be captured already with the eb-MFCC-MBE(2) scheme.