标题
Resolving the complex role of enzyme conformational dynamics in catalytic function
作者
关键词
-
出版物
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 15, Pages 5699-5704
出版商
Proceedings of the National Academy of Sciences
发表日期
2012-03-27
DOI
10.1073/pnas.1117060109
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Extracting Realistic Kinetics of Rare Activated Processes from Accelerated Molecular Dynamics Using Kramers’ Theory
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- Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions
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- A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis
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- Enzyme dynamics point to stepwise conformational selection in catalysis
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- Hidden alternative structures of proline isomerase essential for catalysis
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- Enzyme millisecond conformational dynamics do not catalyze the chemical step
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- A unified model of protein dynamics
- (2009) H. Frauenfelder et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Two-Dimensional Reaction Free Energy Surfaces of Catalytic Reaction: Effects of Protein Conformational Dynamics on Enzyme Catalysis†
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