Atomic insight into short helical peptide comprised of consecutive multiple aromatic residues

The occurrence of sequential multiple aromatic residues in a helical sequence is rare compared to the beta-sheet rich structure. Here, using helix promoting alpha-aminoisobutyric acid (Aib) residues, we unravel atomistic details of the helical secondary structure formation and the super helical assembly of two heptapeptides composed of sequential five and six phenylalanine (Phe) residues.

Automated summary

In this study, the atomistic details of helical secondary structure formation and super helical assembly of two heptapeptides composed of sequentially arranged Phe residues were revealed using helix promoting Aib residues.