Average parameters
Summarise fitted values across replicates and selected experiments.
Across experiments
Move beyond individual fits. See the bigger thermodynamic picture.
FT-ITC Analysis brings related experiments together for global fitting, temperature evaluation and advanced thermodynamic interpretation.
The analysis result
One place to review the result across your experiments.
Move from individual fits to a result that makes the relationship between experiments legible. Review shared and experiment-specific parameters, fit quality and residuals without losing the underlying datasets.
Temperature evaluation
Examine temperature-dependent behaviour and derived relationships such as ΔCp.
Traceable context
Keep the experiments, assumptions and model choices linked to the final result so you can see how each conclusion was reached.
Advanced interpretation
Uncover hidden patterns and relationships in your data through sophisticated analysis techniques.
Global analysis
Fit related experiments as one connected model.
Optimise multiple isotherms simultaneously, decide which parameters are shared, and keep other parameters experiment-specific where that is scientifically appropriate.
Combine datasets
Analyse experiments collected across temperatures, buffers, salt conditions or replicates as one connected result.
Set meaningful constraints
Share selected parameters or connect them through physical relationships while retaining experiment-level values where needed.
Review the evidence
Read global parameters together with individual isotherms, residuals and the experiments contributing to the fit.
Advanced analyses
Ask more of your data.
Beyond affinity and enthalpy, carefully chosen series can unravel the underlying thermodynamics.
Conformational entropy & structuring
Temperature-dependent binding measurements can reveal how enthalpy and entropy change across a series. FT-ITC Analysis brings these results together to examine the conformational entropy and structural change associated with binding.
The workflow is based on the Spolar-Record approach: it uses the temperature dependence of binding thermodynamics, including heat-capacity change, to provide a literature-led view of coupled folding and binding. It is a core advanced feature, but its conclusions should always be read with the experimental design and assumptions in view.
Salt dependence
Compare a series across ionic strengths to evaluate salt effects on binding and estimate the selected model's extrapolated dissociation constant at zero ionic strength.
Proton linkage
Compare titrations performed in buffers with different protonation enthalpies to investigate proton-linked effects on binding.
Further reading
Advanced interpretation starts with the literature.
Read the underlying methods and review the assumptions before drawing specialised conclusions.
Conformational entropy & structuring
1994
Coupling of local folding to site-specific binding of proteins to DNAR. S. Spolar & M. T. Record Jr. · Science 263, 777–784 · DOI 10.1126/science.8303294
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2021Quantification of Conformational Entropy Unravels Effect of Disordered Flanking Region in Coupled Folding and BindingF. F. Theisen et al. · JACS 143, 14540–14550 · DOI 10.1021/jacs.1c04214
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Salt dependence
1990
Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acidsD. P. Mascotti & T. M. Lohman · PNAS 87, 3142–3146 · DOI 10.1073/pnas.87.8.3142
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1976Ion effects on ligand-nucleic acid interactionsM. T. Record Jr., T. M. Lohman & P. de Haseth · Journal of Molecular Biology 107, 145–158 · DOI 10.1016/S0022-2836(76)80023-X
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