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Keywords:

  • G-quadruplexes;
  • hydrates;
  • molecular crowding;
  • thermodynamics;
  • thrombin
Thumbnail image of graphical abstract

Taking on water: The thermodynamics of G-quadruplex–protein binding were investigated for a thrombin-binding DNA aptamer (TBA) and thrombin under the molecular crowding condition of PEG 200. The binding affinity of the TBA–thrombin interaction decreased with a increasing PEG 200 concentration that decreased the water activity. This work suggests that water molecules are taken up during G-quadruplex–protein binding.