title: [Partially unfolded state of lysozyme with a developed secondary structure in dimethylsulfoxide].
abstract: The conformation of a chicken egg lysozyme molecule (dimensions, stoichiometry of its associates, and the degree of helicity) in DMSO was studied by small-angle neutron scattering, dynamic light scattering, and optical rotatory dispersion in the visible region of the spectrum. At high DMSO concentrations (70%), the protein was shown to exist as a dimer. The monomer molecules in the dimer adopt a partially unfolded conformation, with dimensions substantially greater than those in the native state and a high content of secondary structure (the degree of helicity is close to that of native lysozyme). This approach provides a unique possibility to assess the compactness of molecules in associates, which may be very useful in studying protein self-organization.
authors.forename: A A
authors.initials: AA
authors.lastname: Timchenko
authors.forename: M D
authors.initials: MD
authors.lastname: Kirkitadze
authors.forename: D A
authors.initials: DA
authors.lastname: Prokhorov
authors.forename: S A
authors.initials: SA
authors.lastname: Potekhin
authors.forename: I N
authors.initials: IN
authors.lastname: Serdiuk
mesh_terms: D000818:Animals; D002645:Chickens; D004121:Dimethyl Sulfoxide / Q000737:chemistry*; D008027:Light; D009113:Muramidase / Q000737:chemistry*; D009502:Neutrons; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation
chemical_list: D009113:Muramidase; D004121:Dimethyl Sulfoxide
vernacular_title: Chastichno razvernutoe sostoianie lizotsima s razvitoĭ vtorichnoĭ strukturoĭ v dimetilsul'fokside.