Simulation of urea-induced protein unfolding: A lesson from bovine beta-lactoglobulin (Articolo in rivista)

Type

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

Label

• Simulation of urea-induced protein unfolding: A lesson from bovine beta-lactoglobulin (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.jmgm.2011.06.004 (literal)

Alternative label

• Eberini, Ivano; Emerson, Andrew P J; Sensi, Cristina; Ragona, Laura; Ricchiuto, Piero; Pedretti, Alessandro; Gianazza, Elisabetta; Tramontano, Anna (2011)
  Simulation of urea-induced protein unfolding: A lesson from bovine beta-lactoglobulin
  in Journal of molecular graphics & modelling
  (literal)

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

• Eberini, Ivano; Emerson, Andrew P J; Sensi, Cristina; Ragona, Laura; Ricchiuto, Piero; Pedretti, Alessandro; Gianazza, Elisabetta; Tramontano, Anna (literal)

Pagina inizio

• 24 (literal)

Pagina fine

• 30 (literal)

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

• http://www.scopus.com/record/display.url?eid=2-s2.0-84855298578&origin=inward (literal)

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

• 30 (literal)

Rivista

• Journal of molecular graphics & modelling (Rivista)

Note

• Scopu (literal)

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

• Universita degli Studi di Milano; CINECA; Consiglio Nazionale delle Ricerche; Universita degli Studi di Roma La Sapienza (literal)

Titolo

• Simulation of urea-induced protein unfolding: A lesson from bovine beta-lactoglobulin (literal)

Abstract

• To investigate the molecular mechanisms involved in the very initial stages of protein unfolding, we carried out one long (1?s) simulation of bovine ?-lactoglobulin (BLG) together with three (500 ns) supporting MD runs, in which the unfolding conditions were produced by adding the osmolyte urea to the simulated systems and/or by increasing the thermal energy raising the temperature from 300 to 350 K. BLG was chosen, since it is a well-characterized model protein, for which structural and folding properties have been widely investigated by X-ray and NMR. MD trajectories were analyzed not only in terms of standard progress variables, such as backbone H-bonds, gyration radius width, secondary structure elements, but also through the scrutiny of interactions and dynamical behavior of specific key residues previously pointed out and investigated by NMR and belonging to a well known hydrophobic cluster. MD trajectories simulated in different unfolding conditions suggest that urea destabilizes BLG structure weakening protein::protein hydrophobic interactions and the hydrogen bond network. The early unfolding events, better observed at higher temperature, affect both secondary and tertiary structure of the protein. © 2011 Elsevier Inc. All rights reserved. (literal)

Prodotto di

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

Autore CNR

• LAURA GIUDITTA RAGONA (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Simulation of urea-induced protein unfolding: A lesson from bovine beta-lactoglobulin" (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

• Journal of molecular graphics & modelling (Rivista)

Insieme di parole chiave di

• Keywords of "Simulation of urea-induced protein unfolding: A lesson from bovine beta-lactoglobulin" (Insieme di parole chiave)