Crystal structure analysis of helix–turn–helix type motifs in α,γ-hybrid peptides.

Autor: Nalawade, Sachin A., Kumar, Mothukuri Ganesh, Puneeth Kumar, DRGKoppalu R., Singh, Manjeet, Dey, Sanjit, Gopi, Hosahudya N.
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Zdroj: CrystEngComm; 2/21/2024, Vol. 26 Issue 7, p913-917, 5p
Abstrakt: Mimicking protein supersecondary structures using short synthetic peptide sequences holds significant importance in the fields of synthetic protein design, catalysis, and drug discovery. In this study, we present a series of helix–turn–helix motifs derived from short α,γ-hybrid peptides, incorporating centrally positioned E-α,β-unsaturated γ-amino acids. By varying the number of trans double bonds at the central residue, the positioning of the helices can be adjusted. Superimposing the synthetic seven-residue helix–turn–helix motif with the natural calcium-binding helix–turn–helix motif revealed the potential to design three-dimensional helix–turn–helix motifs within short peptide sequences. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index