12 Application of Isothermal Titration Calorimetry (ITC) to Biomolecular Interactions
Graeme L. Conn
Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, USA
12.1 Introduction
12.1.1 Why Measure Binding of Biological Molecules?
Proteins, nucleic acids (DNA and RNA) and other biomolecules do not work in isolation. Rather, the many biological functions of these molecules are defined by their often complex networks of intermolecular exchanges with a diverse array of other biomolecules and bioactive ligands. Enzymes and macromolecular machines like the ribosome, for example, must specifically assemble all required subunits, essential co‐enzymes and/or co‐substrates in order to efficiently catalyse turnover of their bound substrates. Further, enzyme activity may be controlled or localised through interaction with other regulatory binding partners. Similarly, biomolecules that play structural or transport roles in the cell must precisely associate to form their complex macromolecular assemblies. More broadly, regulation of cellular processes from genome replication and stability to each step of gene expression involves a complex and precisely coordinated collection of biomolecular interactions. As a result, understanding what drives biomolecular interactions is at the basis of understanding biology itself.
12.1.2 Approaches for Analysis of Biomolecular Interactions
Many approaches are available to study biomolecular interactions, each with ...