Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 2003.06a
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- Pages.62-62
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- 2003
Elucidation of Serpin's Conformational Switch Mechanism By Rapid Kinetic Study
- Kang, Un-Beom (Functional Proteomics Center, Korea Institute of Science and Technology) ;
- Lee, Cheolju (Life sciences division, Korea Institute of Science and Technology) ;
- Baek, Je-Hyun (Functional Proteomics Center, Korea Institute of Science and Technology) ;
- Seunghyun Ryu (Functional Proteomics Center, Korea Institute of Science and Technology) ;
- Kim, Joon (Laboratory of Biochemistry, Department of Life Science & Biotechnology, Korea University) ;
- Yu, Myeong-Hee (Functional Proteomics Center, Korea Institute of Science and Technology)
- Published : 2003.06.01
Abstract
The native form of serpin (serine protease inhibitor) is kinetically trapped in metastable state. Metastability in these proteins is critical to their biological function. Serpins inhibit target proteases by forming a stable covalent complex in which the cleaved reactive site loop of the serpin is inserted into
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