Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners
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 w...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-09-01
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| Series: | Atmosphere |
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| Online Access: | https://www.mdpi.com/2073-4433/13/9/1448 |
| _version_ | 1797491362472394752 |
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| author | Sahin Uyaver |
| author_facet | Sahin Uyaver |
| author_sort | Sahin Uyaver |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T00:46:24Z |
| format | Article |
| id | doaj.art-b3d01fb52c7144d5ab0dfc518d8be812 |
| institution | Directory Open Access Journal |
| issn | 2073-4433 |
| language | English |
| last_indexed | 2024-03-10T00:46:24Z |
| publishDate | 2022-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Atmosphere |
| spelling | doaj.art-b3d01fb52c7144d5ab0dfc518d8be8122023-11-23T14:59:44ZengMDPI AGAtmosphere2073-44332022-09-01139144810.3390/atmos13091448Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different MannersSahin Uyaver0Department of Energy Science and Technologies, Turkish-German University, Istanbul 34820, TurkeyPhenylalanine, 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.https://www.mdpi.com/2073-4433/13/9/1448aromatic amino acidsaggregationnanostructuresmolecular dynamics |
| spellingShingle | Sahin Uyaver Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners Atmosphere aromatic amino acids aggregation nanostructures molecular dynamics |
| title | Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners |
| title_full | Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners |
| title_fullStr | Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners |
| title_full_unstemmed | Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners |
| title_short | Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners |
| title_sort | tyrosine phenylalanine and tryptophan undergo self aggregation in similar and different manners |
| topic | aromatic amino acids aggregation nanostructures molecular dynamics |
| url | https://www.mdpi.com/2073-4433/13/9/1448 |
| work_keys_str_mv | AT sahinuyaver tyrosinephenylalanineandtryptophanundergoselfaggregationinsimilaranddifferentmanners |