Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin (Articolo in rivista)

Type

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

Label

• Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin (Articolo in rivista) (literal)

Anno

• 2001-01-01T00:00:00+01:00 (literal)

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

• 10.1046/j.1432-1327.2001.02371.x (literal)

Alternative label

• Ugolini, R and Ragona, L and Silletti, E and Fogolari, F and Visschers, RW and Alting, AC and Molinari, H (2001)
  Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin
  in European journal of biochemistry (Print)
  (literal)

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

• Ugolini, R and Ragona, L and Silletti, E and Fogolari, F and Visschers, RW and Alting, AC and Molinari, H (literal)

Pagina inizio

• 4477 (literal)

Pagina fine

• 4488 (literal)

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

• 268 (literal)

Rivista

• European journal of biochemistry (Rivista)

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

• 16 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Molinari, H (Reprint Author), Univ Verona, Dipartimento Sci & Tecnol, Str Grazie 15, I-37134 Verona, Italy. Univ Verona, Dipartimento Sci & Tecnol, I-37134 Verona, Italy. CNR, Ist Chim Macromol, Lab NMR, I-20133 Milan, Italy. Wageningen Ctr Food Sci, Wageningen, Netherlands. NIZO Food Res, Ede, Netherlands. (literal)

Titolo

• Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin (literal)

Abstract

• The study of homologous proteins belonging to the same family can provide a rationale for important molecular properties such as oligomer formation, folding mechanism and mode of binding. We report here a physico-chemical characterization of porcine beta -lactoglobulin, purified from pooled milk: size-exclusion chromatography, CD and NMR measurements were used to study the aggregation and stability of this protein. In spite of the high sequence identity and homology of porcine beta -lactoglobulin with the widely studied bovine species, the two proteins exhibit very different behaviours. The porcine protein shows a monomer-dimer equilibrium with a pH dependence opposite to that observed for the bovine species. Unfolding experiments revealed the presence of an intermediate that probably has excess alpha helices, as reported for equine species. Modelling studies were performed on bovine, porcine and equine proteins, and, interestingly, electrostatic surface potential calculations led to results consistent with the different dimer interface found for porcine beta -lactoglobulin in the crystal structure. Interaction studies revealed that porcine beta -lactoglobulin is unable to bind fatty acids at any pH, thus questioning the main functional role proposed for lactoglobulins as fatty acid transporters or solubilizers. (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 "Dimerization, stability and electrostatic properties of porcine 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

• European journal of biochemistry (Rivista)

Insieme di parole chiave di

• Keywords of "Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin" (Insieme di parole chiave)