AFFINImeter: A software to analyze molecular recognition processes from experimental data

Anal Biochem. 2019 Jul 15:577:117-134. doi: 10.1016/j.ab.2019.02.031. Epub 2019 Mar 5.

Abstract

The comprehension of molecular recognition phenomena demands the understanding of the energetic and kinetic processes involved. General equations valid for the thermodynamic analysis of any observable that is assessed as a function of the concentration of the involved compounds are described, together with their implementation in the AFFINImeter software. Here, a maximum of three different molecular species that can interact with each other to form an enormous variety of supramolecular complexes are considered. The corrections currently employed to take into account the effects of dilution, volume displacement, concentration errors and those due to external factors, especially in the case of ITC measurements, are included. The methods used to fit the model parameters to the experimental data, and to generate the uncertainties are described in detail. A simulation tool and the so called kinITC analysis to get kinetic information from calorimetric experiments are also presented. An example of how to take advantage of the AFFINImeter software for the global multi-temperature analysis of a system exhibiting cooperative 1:2 interactions is presented and the results are compared with data previously published. Some useful recommendations for the analysis of experiments aimed at studying molecular interactions are provided.

Keywords: Affinity; Analysis software; Isothermal titration calorimetry; Kinetics; Molecular recognition; Thermodynamics.

MeSH terms

  • Biophysical Phenomena
  • Calorimetry / methods*
  • Kinetics
  • Protein Binding
  • Proteins / chemistry*
  • Software*
  • Temperature
  • Thermodynamics

Substances

  • Proteins