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Two-dimensional IR correlation spectroscopy of mutants of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events
ArticleAbstract: β-Glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus is a homotetramer with a hPalabras claves:Protein structure, Quaternary structure, Sulfolobus solfataricus, Thermal stability, Two-dimensional infrared spectroscopy, β-glycosidaseAutores:Alessio Ausili, Bertoli E., Cobucci-Ponzano B., Di Lauro B., Moracci M., Rossi M., Scirè A., Tanfani F.Fuentes:googlescopusStructural basis of the destabilization produced by an amino-terminal tag in the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus
ArticleAbstract: We have previously shown that the major ion-pairs network of the tetrameric β-glycosidase from the hPalabras claves:Archaea, Glycoside hydrolase, Infrared spectroscopy, Quaternary structure, Thermal stabilityAutores:Alessio Ausili, Cobucci-Ponzano B., D'Avino R., Di Lauro B., Moracci M., Rossi M., Scirè A., Tanfani F.Fuentes:googlescopus