http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8678
Structural basis of the destabilization produced by an amino-terminal tag in the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus (Articolo in rivista)
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- Structural basis of the destabilization produced by an amino-terminal tag in the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus (Articolo in rivista) (literal)
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- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.biochi.2006.01.009 (literal)
- Alternative label
Ausili A.; Cobucci-Ponzano B.; Di Lauro B.; D'Avino R.; Scire A .; Rossi M.; Tanfani F.; Moracci M. (2006)
Structural basis of the destabilization produced by an amino-terminal tag in the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus
in Biochimie (Print); Elsevier France - Editions Scientifiques Medicales Elsevier, Paris (Francia)
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- Ausili A.; Cobucci-Ponzano B.; Di Lauro B.; D'Avino R.; Scire A .; Rossi M.; Tanfani F.; Moracci M. (literal)
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- Institute of Biochemistry, Università Politecnica delle Marche, Via Ranieri, 60131 Ancona, Italy
Institute of Protein Biochemistry, CNR, Via P.-Castellino 111, 80131 Naples, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico-II, Via Cinthia 4, 80126 Naples, Italy (literal)
- Titolo
- Structural basis of the destabilization produced by an amino-terminal tag in the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus (literal)
- Abstract
- We have previously shown that the major ion-pairs network of the tetrameric â-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus involves more than 16 ion-pairs and hydrogen bonds between several residues from the four subunits and protects the protein from thermal unfolding by sewing the carboxy-termini of the enzyme. We show here that the amino-terminal of the enzyme also plays a relevant role in the thermostabilization of the protein. In fact, the addition of four extra amino acids at the amino-terminal of the â-glycosidase, though not affecting the catalytic machinery of the enzyme and its thermophilicity, produced a faster enzyme inactivation in the temperature range 8595 °C and decreased the Tm of the protein of 6 °C, measured by infrared spectroscopy. In addition, detailed two-dimensional IR correlation analysis revealed that the quaternary structure of the tagged enzyme is destabilized at 85 °C whilst that of the wild type enzyme is stable up to 98 °C. Molecular models allowed the rationalization of the experimental data indicating that the longer amino-terminal tail may destabilize the â-glycosidase by enhancing the molecular fraying of the polypeptide and loosening the dimeric interfaces. The data support the hypothesis that fraying of the polypeptide chain termini is a relevant event in protein unfolding. (literal)
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