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, -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 (see figure).
Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide
Diana D;Colombo G;Pedone C;D'Andrea LD
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, -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 (see figure).File in questo prodotto:
| File | Dimensione | Formato | |
|---|---|---|---|
|
prod_169201-doc_21206.pdf
non disponibili
Descrizione: Articolo su rivista
Dimensione
377.82 kB
Formato
Adobe PDF
|
377.82 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
