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Contributo in rivista
Tipo: Articolo in rivista
Titolo: Stability and dynamics of the porcine odorant-binding protein
Anno di pubblicazione: 2007
Autori: Staiano M.; D'Auria S.; Varriale A.; Rossi M.; Marabotti A.; Fini C.; Stepanenko O.V.; Kuznetsova I.M.; Turoverov K.K.
Affiliazioni autori: Institute of Protein Biochemistry, CNR, Naples, Italy, Institute of Food Sciences, CNR, AVellino, Italy, University of Perugia, Italy, and Institute of Cytology, RAS, St. Petersburg, Russia
Abstract: The denaturation process of porcine odorant-binding protein (pOBP) was studied by intrinsic fluorescence analysis and far- and near-UV circular dichroism measurements. Our results showed that a reversible one-step process described the denaturation by GdnHCl. The midpoint of the transition, that is, the point where the free energies of protein in the native and unfolded states are equal, corresponds to 2.3 M GdnHCl. The difference in free energy between native and unfolded states of pOBP is -5.95 kcal/mol in the absence of GdnHCl, indicating that the protein molecule is very stable to the denaturing action of GdnHCl. A 15% increase in fluorescence intensity accompanied by a 25% decrease of fluorescence decay lifetime recorded in the range of 0.0-1.4 M GdnHCl was explained by the destruction of the complex between Trp 16 and the positively charged atom NZ of Lys 120, localized over the center of the Trp 16 indole ring, with concurrent formation of complex between Trp 16 and bound water molecules also located in its close vicinity.
Lingua abstract: inglese
Pagine da: 11120
Pagine a: 11127
American Chemical Society.
Numero volume: 46
Numero fascicolo: 39
Referee: Sė: Internazionale
Indicizzato da: ISI Web of Science (WOS) 
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