A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli.

@article{Pedone2001ASP,
  title={A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli.},
  author={Emilia Maria Pedone and Michele Saviano and Mos{\'e} Rossi and Simonetta Bartolucci},
  journal={Protein engineering},
  year={2001},
  volume={14 4},
  pages={255-60}
}
Glu85 in the Escherichia coli thioredoxin, which is localized in the loop between beta4 and beta5, was substituted with the Arg present in the corresponding position in Bacillus acidocaldarius thioredoxin. This suggested that it could play an important role in the structure and thermostability of this protein owing to its involvement in numerous interactions. The effects of the mutation on the biophysical properties were analysed by circular dichroism, spectrofluorimetry and limited proteolysis… CONTINUE READING

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of appearance during the timecourse experiments

R. I. Krohn, G. T. Hermanson, +4 authors D. C. Klenk
Biopolymers • 1991

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