Characterization of protein-protein interactions by isothermal titration calorimetry.

Adrian Velazquez-Campoy, Stephanie A. Leavitt, Ernesto I Freire

Research output: Contribution to journalArticle

Abstract

Isothermal titration calorimetry (ITC) is a powerful technique to study both protein-ligand and protein-protein interactions. This methods chapter is devoted to describing protein-protein interactions, in particular, the association between two different proteins and the self-association of a protein into homodimers. ITC is the only technique that determines directly the thermodynamic parameters of a given reaction: DeltaG, DeltaH, DeltaS, and DeltaCP. Isothermal titration calorimeters have evolved over the years and one of the latest models is the VP-ITC produced by Microcal, Inc. In this chapter we will be describing the general procedure for performing an ITC experiment as well as for the specific cases of porcine pancreatic trypsin binding to soybean trypsin inhibitor and the dissociation of bovine pancreatic alpha-chymotrypsin.

Original languageEnglish (US)
Pages (from-to)35-54
Number of pages20
JournalMethods in molecular biology (Clifton, N.J.)
Volume261
StatePublished - 2004

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Calorimetry
Proteins
Aprotinin
Thermodynamics
Soybeans
Trypsin
Swine
Ligands

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Characterization of protein-protein interactions by isothermal titration calorimetry. / Velazquez-Campoy, Adrian; Leavitt, Stephanie A.; Freire, Ernesto I.

In: Methods in molecular biology (Clifton, N.J.), Vol. 261, 2004, p. 35-54.

Research output: Contribution to journalArticle

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