Efecto de surfactantes sobre la estabilidad y actividad catalítica de una proteína de membrana hipertermófila
Membrane proteins represent about 25% - 30% of the total proteins codified in known genomes. However, the Study of their stability has not received as much attention compared to soluble proteins. Despite helical membrane proteins appear to be resistant to chemical denaturation, ionic detergents such...
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| Formato: | Tesis doctoral acceptedVersion |
| Lenguaje: | Español |
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Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica
2020
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| Acceso en línea: | http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=posgraafa&cl=CL1&d=HWA_6415 https://repositoriouba.sisbi.uba.ar/gsdl/collect/posgraafa/index/assoc/HWA_6415.dir/6415.PDF |
| Aporte de: |
| Sumario: | Membrane proteins represent about 25% - 30% of the total proteins codified in known genomes. However, the Study of their stability has not received as much attention compared to soluble proteins. Despite helical membrane proteins appear to be resistant to chemical denaturation, ionic detergents such as SDS have been shown to be efficient denaturants for some of them. It this work, we evaluated the SDS induced denaturation of a Cut(I) transport ATPase of the hyperthermophilic microorganism Archaeoglobus fulgidus. This surfactant was used to characterize the thermodynamic stability of the complete protein and the isolated catalytic domain. The results suggest that the interaction occurs with the presence of multiple intermediaries. The comparative analysis allowed us to propose a mechanism for the denaturation process. |
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