title: [Calorimetric study of G-actin denaturation].
abstract: 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.
mesh_terms: D000199:Actins; D000818:Animals; D002151:Calorimetry / Q000379:methods; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D009206:Myocardium; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D000199:Actins
vernacular_title: Kalorimetrichekoe issledovanie denaturatsii G-aktina.