Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference (한국전기전자재료학회:학술대회논문집)
- 2001.11a
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- Pages.3-6
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- 2001
Conformational Switch and Functional Regulation of Proteins
단백질의 구조 전환과 기능 조절
Abstract
In common globular proteins, the native form is in its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these Proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, and internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of