Thermodynamic analysis of the complexation of quinacrine with tRNAPhe

Thermodynamic analysis of the complexation of quinacrine with tRNAPhe •Thermodynamics of the binding of quinacrine with tRNAphe was studied using ITC.•The binding was exothermic in nature.•The binding was mainly driven by non-polyelectrolytic forces.•Enthalpy-entropy compensation was observed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Chemical Thermodynamics Elsevier

Thermodynamic analysis of the complexation of quinacrine with tRNAPhe

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Publisher
Elsevier
Copyright
Copyright © 2018 Elsevier Ltd
ISSN
0021-9614
eISSN
1096-3626
D.O.I.
10.1016/j.jct.2018.01.002
Publisher site
See Article on Publisher Site

Abstract

•Thermodynamics of the binding of quinacrine with tRNAphe was studied using ITC.•The binding was exothermic in nature.•The binding was mainly driven by non-polyelectrolytic forces.•Enthalpy-entropy compensation was observed.

Journal

The Journal of Chemical ThermodynamicsElsevier

Published: May 1, 2018

References

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