http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13607
Molecular dynamics analyses of cross-b-spine steric zipper models: b-sheet twisting and aggregation (Articolo in rivista)
- Type
- Label
- Molecular dynamics analyses of cross-b-spine steric zipper models: b-sheet twisting and aggregation (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1073/pnas.0602345103 (literal)
- Alternative label
Esposito, Luciana; Pedone, Carlo; Vitagliano, Luigi. (2006)
Molecular dynamics analyses of cross-b-spine steric zipper models: b-sheet twisting and aggregation
in Proceedings of the National Academy of Sciences of the United States of America
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Esposito, Luciana; Pedone, Carlo; Vitagliano, Luigi. (literal)
- Pagina inizio
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
- Pubblicazione su rivista scientifica (literal)
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- CNR Istituto di Biostrutture e Bioimmagini (literal)
- Titolo
- Molecular dynamics analyses of cross-b-spine steric zipper models: b-sheet twisting and aggregation (literal)
- Abstract
- The structural characterization of amyloid fibers is one of the most
investigated areas in structural biology. The structural motif,
denoted as steric zipper, recently discovered for the peptide
GNNQQNY [Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. O.,
Riekel, C., Grothe, R. & Eisenberg, D. (2005) Nature 435, 773-778],
is expected to exert strong influence in this field. To obtain further
insights into the features of this unique structural motif, we report
several molecular dynamics simulations of various GNNQQNY
aggregates. Our analyses show that even pairs of beta?-sheets composed
of a limited number of ?beta-strands are stable in the 20-ns time
interval considered, which suggests that steric zipper interactions
at a ?beta-sheet-?beta-sheet interface strongly contribute to the stability
of these aggregates. Moreover, although the basic features of side
chain-side chain interactions are preserved in the simulation, the
backbone structure undergoes significant variations. Upon equilibration,
a significant twist of the beta?-strands that compose the
beta?-sheets is observed. These results demonstrate that the occurrence
of steric zipper interactions is compatible with flat and
twisted beta?-sheets. Molecular dynamics simulations carried out on
two pairs of beta?-sheets, separated in the crystal state by a hydrated
interface, lead to interesting results. The two pairs of sheets, while
twisting, associate through stable peptide-peptide interactions.
These findings provide insight into the mechanism that leads to the
formation of higher aggregates. On these bases, it is possible to
reconcile the crystallographic and the EM data on the size of the
basic GNNQQNY fiber unit. (literal)
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