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

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Label
  • Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/chem.200800180 (literal)
Alternative label
  • Diana D., Ziaco B., Colombo G., Scarabelli G., Romanelli A., Pedone C., Fattorusso R., D'Andrea L.D. (2008)
    Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide
    in Chemistry - A European Journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Diana D., Ziaco B., Colombo G., Scarabelli G., Romanelli A., Pedone C., Fattorusso R., D'Andrea L.D. (literal)
Pagina inizio
  • 4164 (literal)
Pagina fine
  • 4166 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 14 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 14 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Diana D., Univ Naples 2, Dipartimento Sci Ambientali, I-81100 Caserta, Italy Ziaco B., CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy Colombo G., CNR, Ist Chim Riconoscimento Molecolare, I-20131 Milan, Italy Scarabelli G., CNR, Ist Chim Riconoscimento Molecolare, I-20131 Milan, Italy Romanelli A., Univ Naples Federico 2, Dipartimento Sci Biol, I-80134 Naples, Italy Pedone C., CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy Fattorusso R., Univ Naples 2, Dipartimento Sci Ambientali, I-81100 Caserta, Italy D'Andrea L.D., CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy (literal)
Titolo
  • Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide (literal)
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). (literal)
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