Fiche publication
Date publication
janvier 2012
Journal
Journal of the American Chemical Society
Auteurs
Membres identifiés du Cancéropôle Est :
Dr ENNIFAR Eric
Tous les auteurs :
Burnouf D, Ennifar E, Guedich S, Puffer B, Hoffmann G, Bec G, Disdier F, Baltzinger M, Dumas P
Lien Pubmed
Résumé
Isothermal titration calorimetry (ITC) is the method of choice for obtaining thermodynamic data on a great variety of systems. Here we show that modern ITC apparatus and new processing methods allow researchers to obtain a complete kinetic description of systems more diverse than previously thought, ranging from simple ligand binding to complex RNA folding. We illustrate these new features with a simple case (HIV-1 reverse transcriptase/inhibitor interaction) and with the more complex case of the folding of a riboswitch triggered by the binding of its ligand. The originality of the new kinITC method lies in its ability to dissect, both thermodynamically and kinetically, the two components: primary ligand binding and subsequent RNA folding. We are not aware of another single method that can yield, in a simple way, such deep insight into a composite process. Our study also rationalizes common observations from daily ITC use.
Mots clés
Calorimetry, methods, HIV Reverse Transcriptase, antagonists & inhibitors, HIV-1, enzymology, Kinetics, Nevirapine, metabolism, Reverse Transcriptase Inhibitors, metabolism, Riboswitch, Statistics as Topic, methods, Thermodynamics, Thiamine Pyrophosphate, metabolism
Référence
J. Am. Chem. Soc.. 2012 Jan 11;134(1):559-65
