Metastability in the inhibitory mechanism of human alpha1-antitrypsin.

@article{Im1999MetastabilityIT,
  title={Metastability in the inhibitory mechanism of human alpha1-antitrypsin.},
  author={Hana Im and Eun Joo Seo and Myeong Hee Yu},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 16},
  pages={11072-7}
}
Metastability of the native form of proteins has been recognized as a mechanism of biological regulation. The energy-loaded structure of the fusion protein of influenza virus and the strained native structure of serpins (serine protease inhibitors) are typical examples. To understand the structural basis and functional role of the native metastability of inhibitory serpins, we characterized stabilizing mutations of alpha1-antitrypsin in a region presumably involved in complex formation with a… CONTINUE READING

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