New methods for data analysis of isothermal titration calorimetry Export

@article{citeulike:4036232, abstract = {Heat divided by ligand concentration vs. heat, similar to the Scatchard plot, was introduced to obtain the equilibrium constant (K) and the enthalpy of binding (DeltaH) using isothermal titration calorimetry data. Values of K and DeltaH obtained by this linear pseudo-Scatchard plot for a system with a set of independent binding sites (such as binding fluoride ions on urease and monosaccharide methyl alpha-D-mannopyranoside on concavalin A) were remarkably like that obtained from a normal fitting Wiseman method and other our technical methods. On applying this graphical method to study the binding of copper ion on myelin basic protein (MBP), a concave downward curve obtained was consistent with the positive cooperativity in the binding. A graphical fitting by simple method for determination of thermodynamic parameters was also introduced. This method is general, without any assumption and restriction made in previous method. This general method was applied to the product inhibition study of adenosine deaminase.}, author = {Saboury, A. A.}, citeulike-article-id = {4036232}, journal = {Journal Journal of Thermal Analysis and Calorimetry}, keywords = {itc}, month = {April}, number = {1}, pages = {93--103}, posted-at = {2009-02-11 16:53:39}, priority = {2}, title = {New methods for data analysis of isothermal titration calorimetry}, volume = {72}, year = {2003} }

TY - JOUR ID - citeulike:4036232 L3 - citeulike-article-id:4036232 N2 - Heat divided by ligand concentration vs. heat, similar to the Scatchard plot, was introduced to obtain the equilibrium constant (K) and the enthalpy of binding (DeltaH) using isothermal titration calorimetry data. Values of K and DeltaH obtained by this linear pseudo-Scatchard plot for a system with a set of independent binding sites (such as binding fluoride ions on urease and monosaccharide methyl alpha-D-mannopyranoside on concavalin A) were remarkably like that obtained from a normal fitting Wiseman method and other our technical methods. On applying this graphical method to study the binding of copper ion on myelin basic protein (MBP), a concave downward curve obtained was consistent with the positive cooperativity in the binding. A graphical fitting by simple method for determination of thermodynamic parameters was also introduced. This method is general, without any assumption and restriction made in previous method. This general method was applied to the product inhibition study of adenosine deaminase. IS - 1 JF - Journal Journal of Thermal Analysis and Calorimetry EP - 103 TI - New methods for data analysis of isothermal titration calorimetry VL - 72 SP - 93 KW - itc AU - Saboury, AA PY - 2003/04// ER -