Minimum Free Energy Path of Ligand-Induced Transition in Adenylate Kinase

@inproceedings{Matsunaga2012MinimumFE,
  title={Minimum Free Energy Path of Ligand-Induced Transition in Adenylate Kinase},
  author={Yasuhiro Matsunaga and Hiroshi Fujisaki and Tohru Terada and Tadaomi Furuta and Kei Moritsugu and Akinori Kidera},
  booktitle={PLoS Computational Biology},
  year={2012}
}
Large-scale conformational changes in proteins involve barrier-crossing transitions on the complex free energy surfaces of high-dimensional space. Such rare events cannot be efficiently captured by conventional molecular dynamics simulations. Here we show that, by combining the on-the-fly string method and the multi-state Bennett acceptance ratio (MBAR) method, the free energy profile of a conformational transition pathway in Escherichia coli adenylate kinase can be characterized in a high… CONTINUE READING
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