Abstract
A terminally blocked tripeptide Boc-β-Ala-Aib-β-Ala-OMe 1 with noncoded amino acids forms a novel type of hairpin structure containing a γ-turn instead of a conventional β-turn in the central loop region in solution. This new type structural motif was characterized by NMR and restraint molecular dynamics simulation study. In the solid state peptide 1 adopts an extended backbone conformation and self-assembles to form supramolecular β-sheet.
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Maji, S.K., Haldar, D., Mukhopadhyay, C. et al. Conformational Heterogeneity of a Tripeptide in the Solid State and in Solution: Characterization of a γ-Turn Containing Incipient Hairpin in Solution. Journal of Structural Chemistry 44, 790–795 (2003). https://doi.org/10.1023/B:JORY.0000029816.31278.7b
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DOI: https://doi.org/10.1023/B:JORY.0000029816.31278.7b