| Summary: | Phenylalanine, tyrosine, and tryptophan are aromatic amino acids, and they are of high interest in both health science and biotechnology. These amino acids form organized structures, like fibrils and nanotubes. Although these amino acids belong to the same family, they still differ from each other with respect to polarity, hydrophobicity as well as internal structures. In this work, we performed extensive molecular dynamics simulations to investigate the dynamics of the self-aggregations of these amino acids and studied the details of the formed structures. The amino acid monomers placed in water were simulated at a constant temperature. It has been observed that they compose nanostructures with similarities and differences.
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