Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

@article{Tang2007OpentoclosedTI,
  title={Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR},
  author={Chun Tang and Charles D. Schwieters and G. Marius Clore},
  journal={Nature},
  year={2007},
  volume={449},
  pages={1078-1082}
}
Large-scale domain rearrangements in proteins have long been recognized to have a critical function in ligand binding and recognition, catalysis and regulation. Crystal structures have provided a static picture of the apo (usually open) and holo usually closed) states. The general question arises as to whether the apo state exists as a single species in which the closed state is energetically inaccessible and interdomain rearrangement is induced by ligand or substrate binding, or whether the… Expand
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