Heat and proteins

Authors

Keywords:

calorimetry, proteins, triose phosphate isomerase, Armando Gómez Puyou

Abstract

Calorimetry is a useful technique to study proteins. It allows the measurement of the amount of heat that is released or absorbed when a protein interacts with another substance or when the protein is denatured. In the present article, two types of calorimeters are described: the isothermal titration calorimeter (ITC) and the differential scanning calorimeter (DSC). This text also refers to two projects developed in collaboration with Dr. Armando Gómez Puyou, one where the ITC was employed to reveal the interaction between triosephosphate isomerase and an inhibitor of its catalytic activity, and the other where the DSC was used to study its thermal denaturation.

References

AGUIRRE, B. "A ribosomal misincorporation of Lys for Arg in human triosephosphate isomerase expressed in Escherichia coli gives rise to two protein populations". PLoS ONE, 2011, 6(6): e21035.

COOPER, Alan. Tutorial Chemistry Texts, The Royal Society of Chemistry, 2004.

TÉLLEZ-VALENCIA et al. "Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface". J. Mol. Biol., 2004, 341 (5), 1355-1365.

Published

2017-03-15