Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification.

@article{Kato2000EnthalpicDO,
  title={Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification.},
  author={Akio Kato and S. Nakamura and M Ban and Hiroyuki Azakami and Katsuhide Yutani},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1481 1},
  pages={
          88-96
        }
}
To understand the role of polyglycosylation in protein stability, the thermodynamic changes in the denaturation of various polymannosyl lysozyme mutants (R21T, G49N, R21T/G49N) constructed by genetic modification were analyzed using differential scanning calorimetry (DSC). The denaturation temperature and the enthalpy change for unfolding of the lysozymes were reduced with an increase in the length of the polymannose chain and the number of binding sites to a protein, although the polymannosyl… Expand
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