Engineering a Non-Inhibitory Serpin, Ovalbumin

  • Jeoung, Yeon-Hee (Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology) ;
  • Yu, Myeong-Hee (Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology)
  • Published : 1997.07.01

Abstract

Serpins (serine protease inhibitor) are single polypeptide proteins of around 400 amino acids, and have a conserved secondary structure consisted of three ${\beta}$-sheets and nine ${\alpha}$-helices. Native conformation of inhibitory serpins is a metastable and requires conformational changes to inhibit target protease.(omitted)

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