Phe, Tyr, and Trp: Conformational Study of Ionic and Dimeric Forms

This study presents an in-depth conformational analysis of three aromatic amino acids tryptophan, phenylalanine, and tyrosine along with their ionic and zwitterionic forms, using first-principles calculations. For each amino acid, extensive potential energy surface scans revealed numerous stable conformers, including over 50 unique dimeric structures for each. Stabilization of these structures arises from a rich interplay of noncovalent interactions such as hydrogen bonds (especially NH-O),...