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


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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.

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D. Kaluzhny

Engelhardt Institute of Molecular Biology

编辑信件的主要联系方式.
Email: uzhny@mail.ru
俄罗斯联邦, ul. Vavilova 32, Moscow, 119991

O. Mamaeva

Engelhardt Institute of Molecular Biology

Email: uzhny@mail.ru
俄罗斯联邦, ul. Vavilova 32, Moscow, 119991

A. Beniaminov

Engelhardt Institute of Molecular Biology

Email: uzhny@mail.ru
俄罗斯联邦, ul. Vavilova 32, Moscow, 119991

A. Shchyolkina

Engelhardt Institute of Molecular Biology

Email: uzhny@mail.ru
俄罗斯联邦, ul. Vavilova 32, Moscow, 119991

M. Livshits

Engelhardt Institute of Molecular Biology

Email: uzhny@mail.ru
俄罗斯联邦, ul. Vavilova 32, Moscow, 119991

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