Role of hydration in collagenrecognition by bacterial adhesins (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Role of hydration in collagenrecognition by bacterial adhesins (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.bpj.2011.03.033 (literal)

Alternative label

• Vitagliano L, Berisio R, De Simone A (2011)
  Role of hydration in collagenrecognition by bacterial adhesins
  in Biophysical journal (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Vitagliano L, Berisio R, De Simone A (literal)

Pagina inizio

• 2253 (literal)

Pagina fine

• 2261 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 100 (literal)

Rivista

• Biophysical journal (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 9 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 9 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerce (IBB-CNR), Naples, Italy (literal)

Titolo

• Role of hydration in collagenrecognition by bacterial adhesins (literal)

Abstract

• Protein-protein recognition regulates the vast majority of physiological or pathological processes. We investigated the role of hydration in collagen recognition by bacterial adhesin CNA by means of first principle molecular-dynamics samplings. Our characterization of the hydration properties of the isolated partners highlights dewetting-prone areas on the surface of CNA that closely match the key regions involved in hydrophobic intermolecular interactions upon complex formation, suggesting that the hydration state of the ligand-free CNA predisposes the protein to the collagen recognition. Moreover, hydration maps of the CNA-collagen complex reveal the presence of a number of structured water molecules that mediate intermolecular interactions at the interface between the two proteins. These hydration sites feature long residence times, significant binding free energies, and a geometrical distribution that closely resembles the hydration pattern of the isolated collagen triple helix. These findings are striking evidence that CNA recognizes the collagen triple helix as a hydrated molecule. For this structural motif, the exposure of several unsatisfied backbone carbonyl groups results in a strong interplay with the solvent, which is shown to also play a role in collagen recognition (literal)

Prodotto di

• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• LUIGI VITAGLIANO (Persona)
• RITA BERISIO (Unità di personale interno)

Incoming links:

Autore CNR di

• LUIGI VITAGLIANO (Persona)
• RITA BERISIO (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biophysical journal (Rivista)