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Amino 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:googlescopusEngineering a switch-based biosensor for arginine using a Thermotoga maritima periplasmic binding protein
ArticleAbstract: The Thermotoga maritima arginine-binding protein (TmArgBP) has been modified to create a reagentlessPalabras claves:Fluorescence, Hyperthermophilic bacteria, Periplasmic binding protein, Photo-induced electron transfer, Switch-based biosensorAutores:Alessio Ausili, Billones H., Dattelbaum J., Deacon L., Donaldson T., D’auria S., Iozzino L.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