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Binding of glucose to the D-galactose/D-glucose-binding protein from Escherichia coli restores the native protein secondary structure and thermostability that are lost upon calcium depletion
ArticleAbstract: The effect of the depletion of calcium on the structure and thermal stability of the D-galactose/D-gPalabras claves:Galactose/glucose-binding protein, Infrared spectroscopy, Protein stability, Protein structureAutores:Alessio Ausili, Bertoli E., D’auria S., Marabotti A., Rossi M., Scognamiglio V., Staiano M., Tanfani F., Varriale A.Fuentes:googlescopusCorrelation between fluorescence and structure in the orange-emitting GFP-like protein, monomeric Kusabira Orange
ArticleAbstract: The mKO is the monomeric version of Kusabira Orange, a GFP-like protein emitting bright orange fluorPalabras claves:Fluorescent proteins, FTIR, mKO, Protein structure, Thermo-stabilityAutores:Alessio Ausili, D'Auria G., D’auria S., Gómez‐Fernández J.C., Marabotti A., Ortiz A., Staiano M., Torrecillas A.Fuentes:googlescopusAmino acid transport in thermophiles: Characterization of an arginine-binding protein from Thermotoga maritima. 3. Conformational dynamics and stability
ArticleAbstract: Arginine-binding protein from Thermotoga maritima (TmArgBP) is a 27.7 kDa protein possessing the typPalabras claves:arginine, extremophiles, Fluorescence, Phosphorescence, Thermodynamics, UnfoldingAutores:Alessio Ausili, Dattelbaum J., D’auria S., Fessas D., Pennacchio A., Schiraldi A., Staiano M.Fuentes:googlescopusPeriplasmic binding proteins in thermophiles: Characterization and potential application of an arginine-binding protein from Thermotoga maritima: A brief thermo-story
ReviewAbstract: Arginine-binding protein from the extremophile Thermotoga maritima is a 27.7 kDa protein possessingPalabras claves:ABC transporters, arginine, Periplasmic binding proteins, Structural stability, UnfoldingAutores:Alessio Ausili, Capo A., Dattelbaum J., D’auria S., Staiano M., Varriale A.Fuentes:googlescopus