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Hydration is Required in DNA G‐Quadruplex–Protein Binding
Author(s) -
Nagatoishi Satoru,
Isono Noburu,
Tsumoto Kouhei,
Sugimoto Naoki
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100264
Subject(s) - aptamer , g quadruplex , dna , thrombin , chemistry , scatchard plot , computational biology , biophysics , biochemistry , combinatorial chemistry , binding site , microbiology and biotechnology , biology , platelet , immunology
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.
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