Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases (Articolo in rivista)

Type

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

Label

• Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases (Articolo in rivista) (literal)

Anno

• 2002-01-01T00:00:00+01:00 (literal)

Alternative label

• Del Vecchio P., Graziano G., Granata V., Barone G., Mandrich L., Rossi M., Manco G. (2002)
  Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases
  in Biochemical journal (Lond., 1984)
  (literal)

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

• Del Vecchio P., Graziano G., Granata V., Barone G., Mandrich L., Rossi M., Manco G. (literal)

Pagina inizio

• 857 (literal)

Pagina fine

• 863 (literal)

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

• 367 (literal)

Rivista

• Biochemical journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases (literal)

Abstract

• The stability of two thermophilic esterases, AFEST from Archaeoglobus fulgidus and EST2 from Alicyclobacillus acidocaldarius, against the denaturing action of urea and guanidine hydrochloride has been investigated by means of steady-state fluorescence and circular dichroism measurements. Experimental results indicate that the two enzymes, even though very resistant to temperature and urea, show a resistance to guanidine hydrochloride weaker than expected on the basis of data collected so far for a large set of globular proteins. Structural information available for AFEST and EST2 and ideas that emerged from studies on the molecular origin of the greater thermal stability of thermophiles allow the suggestion of a reliable rationale. The present results may be an indication that the optimization of charge-charge interactions on the protein surface is a key factor for the stability of the two esterases. (literal)

Prodotto di

• Institute of protein biochemistry (IBP) (Istituto)

Autore CNR

• Mosè Rossi (Unità di personale esterno)
• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale esterno)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• Mosè Rossi (Unità di personale esterno)
• LUIGI MANDRICH (Unità di personale esterno)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)

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

• Biochemical journal (Rivista)