한국생물물리학회:학술대회논문집 (Proceedings of the Korean Biophysical Society Conference)

한국생물물리학회 (The Korean Biophysical Society)
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CHARACTERIZATION OF A HUMAN $\alpha_1$-ANTITRYPSIN VARIANT THAT IS AS STABLE AS OVALBUMIN BUT RETAINS INHIBITORY ACTIVITY

  • Lee, Kee-Nyung (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)
  • 발행 : 1996.07.01
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초록

The metastable native state of proteins plays an important role in regulating biological functions. The native strain of serpins (serine protease inhibitors) are considered to be crucial for the inhibitory function. Several thermostable mutations of human $\alpha$$_1$-antitrypsin, a prototype inhibitory serpin, were identified in a systematic search targeted at the hydrophobic core of the molecule [Nature structural biology, vol. 3, no. 6, 497-500(1996)]. (omitted)

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