2011
DOI: 10.1002/cbic.201100264
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Hydration is Required in DNA G‐Quadruplex–Protein Binding

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Cited by 16 publications
(26 citation statements)
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“…As for ligand binding, information regarding hydration changes upon protein binding can be obtained by studying the interaction in the presence of cosolutes. For example, Nagatoishi et al determined the number of water molecules bound upon binding of quadruplex-forming aptamer TBA to thrombin (about 68 water molecules) [46].…”
Section: Studying G-quadruplex Binding Propertiesmentioning
confidence: 99%
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“…As for ligand binding, information regarding hydration changes upon protein binding can be obtained by studying the interaction in the presence of cosolutes. For example, Nagatoishi et al determined the number of water molecules bound upon binding of quadruplex-forming aptamer TBA to thrombin (about 68 water molecules) [46].…”
Section: Studying G-quadruplex Binding Propertiesmentioning
confidence: 99%
“…ITC is a useful tool to study the energetic aspects of G-quadruplexes interaction with ligands and other biomolecules [16], both in the absence and presence of molecular crowding conditions [46]. A typical ITC experiment is carried out by the stepwise addition of one of the component of the complex (e.g.…”
Section: Studying G-quadruplex Binding Propertiesmentioning
confidence: 99%
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“…Water plays a dominant role in guiding the conformational preferences of nucleic acids, as well as in modulating and mediating nucleic acid recognition by small molecules and RNA‐ and DNA‐binding proteins . With respect to G‐quadruplexes, water has been shown to participate in and modulate the thermodynamic stability of G‐quadruplex formation, G‐quadruplex polymorphism, and protein‐G‐quadruplex recognition . Hence, an understanding of the interplay between various molecular forces that govern the polymorphism of G‐quadruplex conformations requires a combination of structural, thermodynamic, and hydration characterizations.…”
Section: Introductionmentioning
confidence: 99%
“…Naoki Sugimoto (Konan University, Japan) demonstrated that thrombin and potassium use different mechanisms to stabilize G4 formation distinguished by specific binding between thrombin and thymine bases within quadruplex loops. Furthermore, water –which may be of limited availability under crowded macromolecular conditions – is required for the binding of thrombin to TBA [14]. Interestingly, water may be more available in the relatively dilute environment of the bloodstream, where thrombin principally functions, consistent with the biological relevance of these findings.…”
Section: Discussionmentioning
confidence: 82%