Conformational constrained β-hairpin peptides are useful tool to modulate protein-protein interactions. A triazole bridge in hydrogen-bonded positions between two antiparallel strands induces a conformational stabilization of the β-hairpin peptide. The entity of the stability of the β-hairpin peptide depends on the length of the bridge.

1,2,3-Triazole Bridge as Conformational Constrain in -Hairpin Peptides: Analysis of Hydrogen-Bonded Positions

FATTORUSSO, Roberto;D'ANDREA, LUCA DOMENICO
2016

Abstract

Conformational constrained β-hairpin peptides are useful tool to modulate protein-protein interactions. A triazole bridge in hydrogen-bonded positions between two antiparallel strands induces a conformational stabilization of the β-hairpin peptide. The entity of the stability of the β-hairpin peptide depends on the length of the bridge.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11591/348581
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