Thermodynamics of unfolding for Kazal-type serine protease inhibitors: entropic stabilization of ovomucoid first domain by glycosylation.

@article{Dekoster1997ThermodynamicsOU,
  title={Thermodynamics of unfolding for Kazal-type serine protease inhibitors: entropic stabilization of ovomucoid first domain by glycosylation.},
  author={Gregory T Dekoster and Andrew D. Robertson},
  journal={Biochemistry},
  year={1997},
  volume={36 8},
  pages={2323-31}
}
A synthetic gene for chicken ovomucoid first domain (OMCHI1) has been overexpressed in Escherichia coli. The resulting recombinant protein, rOMCHI1, is expressed and correctly folded without the use of fusion proteins or export secretion signal peptides incorporated into the gene. The thermostability of rOMCHI1 has been compared to that of the naturally occurring glycosylated OMCHI1 (gOMCHI1). The results of differential scanning calorimetry (DSC) studies show that the heat capacity change for… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

Similar Papers

Loading similar papers…