NMR unfolding studies on a liver bile acid binding protein reveal a global two-state unfolding and localized singular behaviors. (Articolo in rivista)

Type

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

Label

• NMR unfolding studies on a liver bile acid binding protein reveal a global two-state unfolding and localized singular behaviors. (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.abb.2008.10.017 (literal)

Alternative label

• D'Onofrio M.; Ragona L.; Fessas D.; Signorelli M.; Ugolini R.; Pedò M.; Assfalg M.; Molinari H. (2009)
  NMR unfolding studies on a liver bile acid binding protein reveal a global two-state unfolding and localized singular behaviors.
  in Archives of biochemistry and biophysics (Print)
  (literal)

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

• D'Onofrio M.; Ragona L.; Fessas D.; Signorelli M.; Ugolini R.; Pedò M.; Assfalg M.; Molinari H. (literal)

Pagina inizio

• 21 (literal)

Pagina fine

• 29 (literal)

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

• http://www.elsevier.com/locate/yabbi (literal)

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

• 481 (literal)

Rivista

• Archives of biochemistry and biophysics (Rivista)

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

• 1 (literal)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)

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

• D'Onofrio M. - Università di Verona, Ragona L. - Ismac-Milano, Fessas D. - Università di Milano, Signorelli M. - Università di Milano, Ugolini R. - Università di Verona, Pedò M. - Università di Verona, Assfalg M. - Università di Verona, Molinari H. Università di Verona. (literal)

Titolo

• NMR unfolding studies on a liver bile acid binding protein reveal a global two-state unfolding and localized singular behaviors. (literal)

Abstract

• The folding properties of a bile acid binding protein, belonging to a subfamily of the fatty acid binding proteins, have been here investigated both by hydrogen exchange measurements, using the SOFAST NMR approach, and urea denaturation experiments. The urea unfolding profiles of individual residues, acting as single probes, were simultaneously analyzed through a global fit, according to a two-state unfolding model. The resulting conformational stability ?GU(H2O) = 7.2 ± 0.25 kcal mol-1 is in good agreement with hydrogen exchange stability ?Gop. While the majority of protein residues satisfy this model, few amino-acids display a singular behavior, not directly amenable to the presence of a folding intermediate, as reported for other fatty acid binding proteins. These residues are part of a protein patch characterized by enhanced plasticity. To explain this singular behavior a tentative model has been proposed which takes into account the interplay between the dynamic features and the formation of transient aggregates. A functional role for this plasticity, related to translocation across the nuclear membrane, is discussed. (literal)

Prodotto di

• Strutturistica NMR di proteine legate a processi patologici (PM.P01.026.003) (Modulo)
• Istituto per lo studio delle macromolecole (ISMAC) (Istituto)

Autore CNR

• LAURA GIUDITTA RAGONA (Unità di personale interno)

Insieme di parole chiave

• Keywords of "NMR unfolding studies on a liver bile acid binding protein reveal a global two-state unfolding and localized singular behaviors." (Insieme di parole chiave)

Incoming links:

Prodotto

• Istituto per lo studio delle macromolecole (ISMAC) (Istituto)
• Strutturistica NMR di proteine legate a processi patologici (PM.P01.026.003) (Modulo)

Autore CNR di

• LAURA GIUDITTA RAGONA (Unità di personale interno)

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

• Archives of biochemistry and biophysics (Rivista)

Insieme di parole chiave di

• Keywords of "NMR unfolding studies on a liver bile acid binding protein reveal a global two-state unfolding and localized singular behaviors." (Insieme di parole chiave)