A more detailed analysis of the hydrophobic region of the peptides revealed different variants of packing of the flanking side chains of Dip residues 5 and 7, categorized as either non-contacting or closely packed. These two states have rather extended (named as "flat") or more curved ("bend") backbone conformation of the apolar region (Figure ). To distinguish these two modes of packing in the apolar region, we used the distance cutoff of 8 Å between any heavy atoms of the side chains of residues Dip5 and Dip7. No contacts between these side chains within the cutoff were detected for the "flat" conformation, whereas in the "bend" state, side chains of the flanking hydrophobic residues have at least one atom-atom distance that falls within the 8 Å threshold.