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Updated: Jul 13, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Secondary structure binding motifs of the jet cooled tetrapeptide model Ac-Leu-Val-Tyr(Me)-NHMe
H Fricke1, G Schäfer, T Schrader
1Heinrich-Heine Universität Düsseldorf, Institut für Physikalische Chemie I, Universitätsstrasse 26.33.O2, 40225 Düsseldorf, Germany.
Abstract:
In this paper the structure of the isolated tetrapeptide model Ac-Leu-Val-Tyr(Me)-NHMe (Leu = leucine, Val = valine, Tyr = tyrosine) is investigated by mass- and isomer-selective IR/UV double resonance spectroscopy. Two isomers of this peptide are observed and in combination with force field, ab initio, and DFT calculations these structures are assigned to folded arrangements presenting two different secondary structure binding motifs: (a) a combined gamma-turn/beta-turn structure and (b) a triple gamma-turn structure, which is described for the first time for an isolated model system in the gas phase.
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