Electrostatic properties of bovine beta-lactoglobulin (Articolo in rivista)

Type
Label
  • Electrostatic properties of bovine beta-lactoglobulin (Articolo in rivista) (literal)
Anno
  • 2000-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/(SICI)1097-0134(20000601)39:4<317::AID-PROT50>3.0.CO;2-W (literal)
Alternative label
  • Fogolari, F and Ragona, L and Licciardi, S and Romagnoli, S and Michelutti, R and Ugolini, R and Molinari, H (2000)
    Electrostatic properties of bovine beta-lactoglobulin
    in Proteins (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Fogolari, F and Ragona, L and Licciardi, S and Romagnoli, S and Michelutti, R and Ugolini, R and Molinari, H (literal)
Pagina inizio
  • 317 (literal)
Pagina fine
  • 330 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 39 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 4 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Fogolari, F (Reprint Author), Univ Verona, Dipartimento Sci & Tecnol, Ca Vignal 1,Strada Grazie, I-37134 Verona, Italy. Univ Verona, Dipartimento Sci & Tecnol, I-37134 Verona, Italy. CNR, Lab NMR, I-20133 Milan, Italy. (literal)
Titolo
  • Electrostatic properties of bovine beta-lactoglobulin (literal)
Abstract
  • Bovine beta-Lactoglobulin (BLG) has been studied for many decades, but only recently structural data have been obtained, making it possible to simulate its molecular properties. in the present study, electrostatic properties of BLG are investigated theoretically using Poisson-Boltzmann calculations and experimentally following pH titration via NMR. Electrostatic properties are determined for several structural models, including an. ensemble of NMR structures obtained at low pH. The changes in electrostatic forces upon changes in ionic strength, solvent dielectric constant, and pH are calculated and compared with experiments. pH(a)s are computed for all titratable sites and compared with NMR titration data. The analysis of theoretical and experimental results suggests that (1) there may be more than one binding sites for negatively charged ligands; (2) at low pH the core of the molecule is more compact than observed in the structures obtained via restrained molecular dynamics from NMR data, but loop and terminal regions must be disordered. (C) 2000 Wiley-Liss, Inc. (literal)
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