1, 2, 3-Triazole Bridge as Conformational Constrain in beta-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions(565 views) Celentano V, Diana D, Di Salvo C, De Rosa L, Romanelli A, Fattorusso R, D'Andrea LD
Istituto di Biostrutture e Bioimmagini CNR, Via Mezzocannone 16, 80134, Napoli, (Italy)., National University of Ireland, Galway, (Ireland)., Dipartimento di Farmacia, Universita di Napoli "Federico II", Via Mezzocannone 16, 80134, Napoli, (Italy)., Dipartimento di Scienze Ambientali, Biologiche e Farmaceutiche, Seconda Universita di Napoli, Via Vivaldi 46, 81100, Caserta, Napoli, (Italy)., Istituto di Biostrutture e Bioimmagini CNR, Via Mezzocannone 16, 80134, Napoli, (Italy). luca.dandrea@cnr.it.,
References: Not available.
1, 2, 3-Triazole Bridge as Conformational Constrain in beta-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions
Conformational constrained beta-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 beta-hairpin peptide. The entity of the stability of the beta-hairpin peptide depends on the length of the bridge.
1, 2, 3-Triazole Bridge as Conformational Constrain in beta-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions
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