The thermodynamics of binding of low-molecular-weight ligands at extreme tetrads of telomeric G-quadruplexes.

Autor: Kaluzhny, D., Mamaeva, O., Beniaminov, A., Shchyolkina, A., Livshits, M.
Zdroj: Biophysics; Jan2016, Vol. 61 Issue 1, p28-33, 6p
Abstrakt: Ligand binding constants at the 3'- and 5'-ends of a fluorophore-labelled telomeric G-quadruplex structure were determined. The temperature dependence of the fluorescence quenching reflected that of the binding constants, which in turn was determined by the thermodynamic parameters of the formation of a DNA-ligand complex. Since the quenching of fluorescence can only be mediated by proximal ligand binding, this method allows the characterization of complexes at different ligand-binding sites. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index