Producció i caracterització de variants de la regió C-terminal de la ribonucleasa A. Importància d'aquesta regió sobre l'estabilitat de l'enzim

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Bovine pancreatic ribonuclease A (RNase A, EC 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 ​
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