DSC measurements have been performed on human superoxide dismutase (HSOD) and on its mutants on the Glu132 and Glu133 residues which have been alternatively modified to a Gin residue. In both cases, the substitution has dramatic effects on the thermal denaturation of HSOD as evidenced by the calorimetric experiments. In particular, replacement of the Glu residue in position 132 seems to have a greater effect on the stabilization of the protein, highlighting the key role played by this position. All the experimental data are qualitatively explained in terms of interactions between the groups which form the active site channel.
Calorimetric evidences of the different structural role of Glu132 and Glu133 residues in human Superoxide Dismutase
MILARDI D;
1996
Abstract
DSC measurements have been performed on human superoxide dismutase (HSOD) and on its mutants on the Glu132 and Glu133 residues which have been alternatively modified to a Gin residue. In both cases, the substitution has dramatic effects on the thermal denaturation of HSOD as evidenced by the calorimetric experiments. In particular, replacement of the Glu residue in position 132 seems to have a greater effect on the stabilization of the protein, highlighting the key role played by this position. All the experimental data are qualitatively explained in terms of interactions between the groups which form the active site channel.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
