Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2 (Abstract/Poster in convegno)

Type

• Abstract/Poster in convegno (Classe)
• Prodotto della ricerca (Classe)

Label

• Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2 (Abstract/Poster in convegno) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

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

• 10.1093/PROTEIN/GZS066 (literal)

Alternative label

• PEZZULLO M., DEL VECCHIO P., MANDRICH L., NCCI R., ROSSI M., MANCO G., (2012)
  Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2
  in 11th International Meeting on Cholinesterases, Kazan, Russia, 4-9 Giugno 2012
  (literal)

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

• PEZZULLO M., DEL VECCHIO P., MANDRICH L., NCCI R., ROSSI M., MANCO G., (literal)

Pagina inizio

• 47 (literal)

Pagina fine

• 58 (literal)

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

• 26 (literal)

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

• 1 (literal)

Note

• Poster (literal)

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

• Istituto di Biochimica delle Proteine, Consiglio Nazionale delle Ricerche (literal)

Titolo

• Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2 (literal)

Abstract

• Here we report a comprehensive analysis through alanine-scanning mutagenesis of the contribution of surface ion pairs to the thermal stability of Alicyclobacillus acidocaldarius esterase 2 (EST2). We produced 16 single mutants, 4 double mutants corresponding to selected ion pairs R31/E118, E43/K102, R58/D130, D145/R148, 2 double mutants (R63A/R98A and E50A/D94A) involving residues of a large ion network on the protein surface and the double-mutant R98A/R148A meant to disrupt the R98 interactions within the said network and, contextually, the interaction between R148 and D145. The double-mutant E43A/E273K was obtained by chance. All selected residues were replaced with alanine except E91, which was mutated to a glycine and K102, which was changed to a glutamine. All 24 proteins were over-expressed in Escherichia coli, purified and characterized with respect to the main features. Structural stability data were compared with an in silico prediction of G values. Our study of the individual factors involved in thermostability and their structural interpretation reveals that the great stability of this thermophilic protein can be explained by the contribution of a few residues at the protein surface. (literal)

Prodotto di

• DR. MANCO : Studi di idrolasi da fonti diverse e proteine vegetali. (SV.P14.010.001) (Modulo)
• Institute of protein biochemistry (IBP) (Istituto)

Autore CNR

• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale interno)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)
• DR. MANCO : Studi di idrolasi da fonti diverse e proteine vegetali. (SV.P14.010.001) (Modulo)

Insieme di parole chiave di

• Keywords of "Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2" (Insieme di parole chiave)