TY - JOUR
T1 - Isothermal titration calorimetry
T2 - application of the gibbs-duhem equation to the study of the relationship between forward and reverse titrations
AU - Grolier, Jean Pierre E.
AU - Del Río, Jose Manuel
N1 - Publisher Copyright:
© 2014 Springer Science+Business Media New York.
PY - 2015/5/1
Y1 - 2015/5/1
N2 - In this work we rigorously demonstrate that, in dilute solutions, the partial enthalpy of interaction of the ligand can be measured by a forward titration and that the partial enthalpy of interaction of the macromolecule with the ligand can be calculated from the Gibbs-Duhem equation. Using a reverse titration, it is possible to experimentally obtain the partial enthalpy of interaction of the macromolecule and to calculate that of the ligand. Based on this fact, we propose a thermodynamic criterion to experimentally discern when the forward process is equal to or different from the reverse process: they are equal (or different) if the interaction partial enthalpies obtained experimentally are equal to (or different from) those calculated from the Gibbs-Duhem equation. The above criterion is applied to four systems taken from the literature. The first system features the interaction between a bilayer and a surfactant. The second system features a binding interaction with two binding sites that are equivalent and independent. The final two systems feature binding interactions with two non-equivalent binding sites.
AB - In this work we rigorously demonstrate that, in dilute solutions, the partial enthalpy of interaction of the ligand can be measured by a forward titration and that the partial enthalpy of interaction of the macromolecule with the ligand can be calculated from the Gibbs-Duhem equation. Using a reverse titration, it is possible to experimentally obtain the partial enthalpy of interaction of the macromolecule and to calculate that of the ligand. Based on this fact, we propose a thermodynamic criterion to experimentally discern when the forward process is equal to or different from the reverse process: they are equal (or different) if the interaction partial enthalpies obtained experimentally are equal to (or different from) those calculated from the Gibbs-Duhem equation. The above criterion is applied to four systems taken from the literature. The first system features the interaction between a bilayer and a surfactant. The second system features a binding interaction with two binding sites that are equivalent and independent. The final two systems feature binding interactions with two non-equivalent binding sites.
KW - Diluted solutions
KW - Forward titration
KW - Isothermal titration calorimetry
KW - Ligand binding
KW - Partial enthalpy
KW - Reverse titration
KW - Thermodynamics
UR - http://www.scopus.com/inward/record.url?scp=84930088581&partnerID=8YFLogxK
U2 - 10.1007/s10953-014-0243-7
DO - 10.1007/s10953-014-0243-7
M3 - Artículo
AN - SCOPUS:84930088581
SN - 0095-9782
VL - 44
SP - 987
EP - 1003
JO - Journal of Solution Chemistry
JF - Journal of Solution Chemistry
IS - 5
ER -