Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide

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 (see figure). Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2111/2008/z800180_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.