Data di Pubblicazione:
2005
Abstract:
The structure, stability, and conformational dynamics of an assembly of two pentameric bundles made of
collagen-like triple helical segments are explored using 1.2 ns molecular dynamics simulations in three
environments: 8.0% (v/v) formaldehyde/water solution, 1.4% (v/v) gallic acid/water solution, and pure water.
Stable supramolecular arrangements, where the two collagen units are very close to each other at interacting
distances, are identified via docking and energy minimization procedures. Analysis of the interaction with
formaldehyde and gallic acid suggests that they perturb the protein in a similar way depending on hydrogenbonding
capability, hydrophobic association properties, and the size and concentration of the compound.
collagen-like triple helical segments are explored using 1.2 ns molecular dynamics simulations in three
environments: 8.0% (v/v) formaldehyde/water solution, 1.4% (v/v) gallic acid/water solution, and pure water.
Stable supramolecular arrangements, where the two collagen units are very close to each other at interacting
distances, are identified via docking and energy minimization procedures. Analysis of the interaction with
formaldehyde and gallic acid suggests that they perturb the protein in a similar way depending on hydrogenbonding
capability, hydrophobic association properties, and the size and concentration of the compound.
Tipologia CRIS:
01.01 Articolo in rivista
Elenco autori:
Cappelli, Chiara; Monti, Susanna; Bronco, Simona
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