期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 104, 期 30, 页码 12253-12258出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0704304104
关键词
protein dynamics; catalysis
资金
- NIGMS NIH HHS [T32 GM008572, T32 GM008572-12, GM068036, P01 GM068036] Funding Source: Medline
The transition path sampling method previously applied in our group to the reaction catalyzed by lactate dehydrogenase was used to generate a transition path ensemble for this reaction. Based on analysis of the reactive trajectories generated, important residues behind the active site were implicated in a compressional motion that brought the donor-acceptor atoms of the hydricle closer together. In addition, residues behind the active site were implicated in a relaxational motion, locking the substrate in product formation. Although this suggested that the compressionrelaxation motions of these residues were important to catalysis, it remained unproven. In this work, we used committor distribution analysis to show that these motions are integral components of the reaction coordinate.
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