Helix stability: Understanding helix stability and formation is a prerequisite to elucidate the mechanism of protein folding and design helix peptides with specific activity. Herein, we analyze the thermal behaviour of a designed, α-helical, bioactive peptide, composed only of natural amino acids. This peptide shows an unusual thermal stability, in which the N-terminal region and a hydrophobic interaction play a major role.
Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide / Diana, D.; Ziaco, B.; Colombo, G.; Scarabelli, G.; Romanelli, Alessandra; Pedone, Carlo; Fattorusso, R.; D’Andrea, L. D.. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - STAMPA. - 14:14(2008), pp. 4164-4166. [10.1002/chem.200800180]
Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide
Diana D.;ROMANELLI, ALESSANDRA;PEDONE, CARLO;
2008
Abstract
Helix stability: Understanding helix stability and formation is a prerequisite to elucidate the mechanism of protein folding and design helix peptides with specific activity. Herein, we analyze the thermal behaviour of a designed, α-helical, bioactive peptide, composed only of natural amino acids. This peptide shows an unusual thermal stability, in which the N-terminal region and a hydrophobic interaction play a major role.| File | Dimensione | Formato | |
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