NMR identification of transient complexes critical to adenylate kinase catalysis.

@article{dn2007NMRIO,
  title={NMR identification of transient complexes critical to adenylate kinase catalysis.},
  author={J{\"o}rgen {\AA}d{\'e}n and Magnus Wolf-Watz},
  journal={Journal of the American Chemical Society},
  year={2007},
  volume={129 45},
  pages={14003-12}
}
A fundamental question in protein chemistry is how the native energy landscape of enzymes enables efficient catalysis of chemical reactions. Adenylate kinase is a small monomeric enzyme that catalyzes the reversible conversion of AMP and ATP into two ADP molecules. Previous structural studies have revealed that substrate binding is accompanied by large rate-limiting spatial displacements of both the ATP and AMP binding motifs. In this report a solution-state NMR approach was used to probe the… CONTINUE READING
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