지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2025.3
- 수록면
- 74 - 80 (7page)
이용수
초록· 키워드
오류제보하기
A model based on elastic body motion is proposed to analyze the changes in enzyme structure induced by substrate binding. The model applies mechanical principles to elucidate the residual forces within the enzyme. Recognizing that the enzyme structure deforms during substrate binding and returns to its original state after product release—analogous to the behavior of elastic materials—a mechanical analysis grounded in Hooke's law was incorporated. Residual forces were determined using the substrate-free and substrate-bound structures of the enzyme. The deformation distance, x, was calculated as the displacement of each residue upon superimposition of these structures. Since no direct tool exists to measure Young’s modulus, k, it was approximated as the inverse of the B-factor, a flexibility indicator derived from X-ray crystallography data. In order to evaluate the model, structural motions of bacteriophage T4 lysozyme, HIV-1 protease and Candida antarctica lipase B were analyzed. Regions of significant force corresponded to areas previously identified as critical for motion or substrate binding in the literature. Additionally, the torque which was calculated by summing the forces in three dimensions, could predict the structural twisting induced by substrate binding.
목차
Abstract
1. INTRODUCTION
2. MATERIALS AND METHODS
3. RESULTS AND DISCUSSION
4. CONCLUSION
REFERENCES
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