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A comparative infrared spectroscopic study of glycoside hydrolases from extremophilic archaea revealed different molecular mechanisms of adaptation to high temperatures
ArticleAbstract: The identification of the determinants of protein thermal stabilization is often pursued by comparinPalabras claves:Infrared, Protein structure, Pyrococcus furiosus, Sulfolobus solfataricus, Thermosphaera aggregans, β-glycosidaseAutores:Alessio Ausili, Bertoli E., Cobucci-Ponzano B., D'Avino R., Di Lauro B., Moracci M., Perugino G., Rossi M., Scirè A., Tanfani F.Fuentes:googlescopusTwo-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:googlescopus