Applications of isothermal titration calorimetry in pure and applied research from 2016 to 2020

Robert J. Falconer*, Boelo Schuur, Anthony K. Mittermaier

*Corresponding author for this work

Research output: Contribution to journalReview articleAcademicpeer-review

Abstract

The last 5 years have seen a series of advances in the application of isothermal titration microcalorimetry (ITC) and interpretation of ITC data. ITC has played an invaluable role in understanding multiprotein complex formation including proteolysis-targeting chimeras (PROTACS), and mitochondrial autophagy receptor Nix interaction with LC3 and GABARAP. It has also helped elucidate complex allosteric communication in protein complexes like trp RNA-binding attenuation protein (TRAP) complex. Advances in kinetics analysis have enabled the calculation of kinetic rate constants from pre-existing ITC data sets. Diverse strategies have also been developed to study enzyme kinetics and enzyme-inhibitor interactions. ITC has also been applied to study small molecule solvent and solute interactions involved in extraction, separation, and purification applications including liquid-liquid separation and extractive distillation. Diverse applications of ITC have been developed from the analysis of protein instability at different temperatures, determination of enzyme kinetics in suspensions of living cells to the adsorption of uremic toxins from aqueous streams.

Original languageEnglish
Article numbere2901
JournalJournal of Molecular Recognition
DOIs
Publication statusE-pub ahead of print/First online - 11 May 2021

Keywords

  • allostery
  • distillation
  • entropy
  • enzyme kinetics
  • kinITC
  • kinITC-ETC
  • liquid-liquid extraction
  • supramolecular

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