Determinants of protein stability and folding: Comparative analysis of beta-lactoglobulins and liver basic fatty acid binding protein (Articolo in rivista)

Type

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

Label

• Determinants of protein stability and folding: Comparative analysis of beta-lactoglobulins and liver basic fatty acid binding protein (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1002/prot.20493 (literal)

Alternative label

• Ragona L., Colombo G., Catalano M., Molinari H. (2005)
  Determinants of protein stability and folding: Comparative analysis of beta-lactoglobulins and liver basic fatty acid binding protein
  in Proteins (Print)
  (literal)

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

• Ragona L., Colombo G., Catalano M., Molinari H. (literal)

Pagina inizio

• 366 (literal)

Pagina fine

• 376 (literal)

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

• 61 (literal)

Rivista

• Proteins (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Ragona, Catalano; molinari:CNR, Lab NMR, ISMAC, I-20133 Milan, Italy Colombo: CNR, Ist Chim Riconoscimento Mol, I-20133 Milan, Italy Molinari: Univ Verona, Dipartimento Sci & Tecnol, I-37134 Verona, Italy (literal)

Titolo

• Determinants of protein stability and folding: Comparative analysis of beta-lactoglobulins and liver basic fatty acid binding protein (literal)

Abstract

• Abstract: A new energy decomposition approach, aimed at identifying residues playing a folding key role, has been applied here to three homologous proteins, belonging to the calycin superfamily, namely bovine and porcine beta-lactoglobulins and Liver basic fatty acid binding protein, sharing the same beta-barrel fold and different degree of sequence identities. All-atom, explicit solvent molecular dynamics simulations around the native conformation were used to generate, for each of the three proteins, energy maps which were further simplified through eigenvalue decomposition. Analysis of the components of the eigenvector associated with the lowest eigenvalue singled out those residues (hot sites) behaving as strongly interacting and possible nucleation centers. The results fit well with experimental folding data and, especially, with the analysis of side chain-side chain interaction conservation. (literal)

Prodotto di

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

Autore CNR

• LAURA GIUDITTA RAGONA (Unità di personale interno)
• GIORGIO COLOMBO (Unità di personale interno)

Incoming links:

Prodotto

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

Autore CNR di

• LAURA GIUDITTA RAGONA (Unità di personale interno)
• GIORGIO COLOMBO (Unità di personale interno)

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

• Proteins (Rivista)