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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:googlescopusA spectroscopic study on secondary structure and thermal unfolding of the plant toxin gelonin confirms some typical structural characteristics and unravels the sequence of thermal unfolding events
ArticleAbstract: Gelonin from the Indian plant Gelonium multiflorum belongs to the type I ribosome-inactivating protePalabras claves:Gelonin, Immunotoxins, Infrared spectroscopy, Ribosome-inactivating protein, Thermal unfolding, Two-dimensional correlation spectroscopyAutores:Alessio Ausili, Scirè A., Tanfani F.Fuentes:googlescopusHigh hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon pyrococcus furiosus. A fourier-transform infrared spectroscopic study
ArticleAbstract: Protein disulfide oxidoreductases (PDOs) are ubiquitous redox enzymes that catalyse dithiol-disulfidPalabras claves:Autores:Alessio Ausili, Baldassarre M., Bartolucci S., Bertoli E., Pedone E., Saviano M., Scirè A., Tanfani F.Fuentes:googlescopusThe thermal unfolding of the ribosome-inactivating protein saporin-S6 characterized by infrared spectroscopy
ArticleAbstract: Abstract Saporin-S6 is a plant toxin belonging to the type 1 ribosome-inactivating protein (RIP) famPalabras claves:Infrared spectroscopy, Ribosome-inactivating protein, Saporin-S6, Thermal unfoldingAutores:A Ausili, A Scir�, Alessio Ausili, F. Tanfani, M. Sánchez, Sánchez M., Scirè A., Tanfani F.Fuentes:googlerraaescopus