http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13337
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (Articolo in rivista)
- Type
- Label
- Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Alternative label
Berisio R., Vitagliano L., Mazzarella L., Zagari A.. (2002)
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
in Protein science (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Berisio R., Vitagliano L., Mazzarella L., Zagari A.. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Titolo
- Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (literal)
- Abstract
- The first report of the full-length structure of the collagen-like
polypeptide [(Pro-Pro-Gly)(10)](3) is given. This structure was obtained
from crystals grown in a microgravity environment, which diffracted up to
1.3 A, using synchrotron radiation. The final model, which was refined to
an R(factor) of 0.18, is the highest-resolution description of a collagen
triple helix reported to date. This structure provides clues regarding a
series of aspects related to collagen triple helix structure and assembly.
The strict dependence of proline puckering on the position inside the
Pro-Pro-Gly triplets and the correlation between backbone and side chain
dihedral angles support the propensity-based mechanism of triple helix
stabilization/destabilization induced by hydroxyproline. Furthermore, the
analysis of [(Pro-Pro-Gly)(10)](3) packing, which is governed by
electrostatic interactions, suggests that charges may act as locking
features in the axial organization of triple helices in the collagen fibrils. (literal)
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- Autore CNR
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