Average parameters
Summarise fitted values across replicates and selected experiments.
Across experiments
See the patterns beyond one titration.
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 contributing experiments, assumptions and model choices close to the result.
Global analysis
Fit related experiments as a connected question.
Optimise multiple isotherms simultaneously, decide which parameters are shared, and keep other parameters experiment-specific where that is scientifically appropriate.
Combine active datasets
Analyse experiments collected across temperatures, buffers, salt conditions or replicates as one connected result.
Set meaningful relationships
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
What changes when binding happens?
When an experiment series is designed for it, FT-ITC Analysis supports additional views of the physical processes behind binding.
Conformational & structuring analysis
Use temperature-dependent binding thermodynamics to examine conformational entropy and the structural change associated with binding. This specialised workflow builds on the Spolar-Record approach and belongs with its assumptions, data and literature context.
Salt dependence
Evaluate ionic-strength effects and estimate the selected model's extrapolated dissociation constant at zero ionic strength.
Proton linkage
Compare titrations across buffers with different protonation enthalpies to investigate linked protonation changes.
Further reading
Advanced interpretation starts with the literature.
Read the underlying methods and review the assumptions before drawing specialised conclusions.
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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