title: [Cold denaturation of staphylococcal nuclease].
abstract: It has been shown that the structure of staphylococcal nuclease breaks down reversibly both at a temperature increase above 20 degrees C and at its decrease. Both the heat and cold denaturations of protein are well approximated by a transition between two states differing in heat capacity, which means that the whole protein molecule represents a unique cooperative system with a well developed hydrophobic core. The transfer to a denatured state at a temperature decrease is accompanied by heat release and leads to a complete loss of the unique tertiary structure, decrease of the helicity and increase of the hydrodynamic volume of the molecule.
authors.forename: Iu V
authors.initials: IuV
authors.lastname: Griko
authors.forename: P L
authors.initials: PL
authors.lastname: Privalov
authors.forename: S Iu
authors.initials: SIu
authors.lastname: Ven'iaminov
mesh_terms: D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003080:Cold Temperature; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008836:Micrococcal Nuclease / Q000032:analysis*; D011489:Protein Denaturation; D014783:Viscosity
chemical_list: D008836:Micrococcal Nuclease
vernacular_title: Kholodovaia denaturatsiia stafilokokkovoĭ nukleazy.