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  • Open Daily: 10am - 10pm
    Alley-side Pickup: 10am - 7pm

    3038 Hennepin Ave Minneapolis, MN
    612-822-4611

Open Daily: 10am - 10pm | Alley-side Pickup: 10am - 7pm
3038 Hennepin Ave Minneapolis, MN
612-822-4611
Phe, Tyr, and Trp: Conformational Study of Ionic and Dimeric Forms

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

Purushotham, Uppula

Paperback

Chemistry

ISBN10: 6208172144
ISBN13: 9786208172145
Publisher: LAP Lambert Academic Publishing
Published: Jul 26 2025
Pages: 120
Weight: 0.38
Height: 0.28 Width: 6.00 Depth: 9.00
Language: English
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), π-π stacking, CH-π, NH-π, and OH-π interactions. Monomeric forms favored conformations with strong intramolecular hydrogen bonding, while dimeric forms demonstrated a balance between hydrogen bonding and aromatic interactions. Atoms-in-molecules analysis provided further insight into the strength and nature of these interactions. Comparative observations with Protein Data Bank structures highlighted geometry-dependent preferences: π-π stacking dominates at close range, while T-shaped CH-π interactions are more prevalent at longer distances. These findings illuminate the intricate noncovalent landscape shaping amino acid conformations in biological systems.

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