Producció i caracterització de variants de la regió C-terminal de la ribonucleasa A. Importància d'aquesta regió sobre l'estabilitat de l'enzim
- Autores: M. Gràcia Coll Constans
- Directores de la Tesis: Maria Vilanova Brugués (dir. tes.)
- Lectura: En la Universitat de Girona ( España ) en 2000
- Idioma: catalán
- Tribunal Calificador de la Tesis: Claudi Miquel Cuchillo Foix (presid.), Antoni Benito Mundet (secret.), José Carreras Barnés (voc.), Alícia Guasch i Mitjans (voc.), M. Victòria Noguès i Bara (voc.)
- Materias:
- Enlaces
- Tesis en acceso abierto en: TDX
- Resumen
Bovine pancreatic ribonuclease A (RNase A, EC 3.1.27.5) has been extensively studied from the structural, mechanistic and functional points of view. Within the protein folding context, it constitutes a good model of study although a rather complicated one due to the presence in the native state of four disulphide bonds and the existence of two X-proline peptide bonds in cis conformation. Most of these studies has focused on the alteration of cysteine or proline residues to study, from a kinetic point of view, the formation of the disulphide bonds or the characterization of the species present in the heterogeneous non-reduced unfolded state, respectively. In these work we have used site-directed mutagenesis to change the characteristics of a postulated chain folding initiation site (CFIS) in RNase A
