Calorimetric study of G-actin denaturation

The investigation of G-actin heat denaturation at various pH of the solution by scanning microcalorimetry has shown that unfolding of G-actin is not a two-state process. Since the protein structure does not behave as a single cooperative unit during heat denaturation, it is suggested that the G-actin globule consists, at least, of two interacting domains.