한국생물물리학회:학술대회논문집 (Proceedings of the Korean Biophysical Society Conference)
- 한국생물물리학회 2003년도 정기총회 및 학술발표회
- /
- Pages.62-62
- /
- 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)
- 발행 : 2003.06.01
초록
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
키워드