title: [Denatured state of lysozyme in dimethyl sulfoxide].
abstract: An influence of DMSO on lysozyme structure in solution was studied by fluorescence and optical rotary dispersion methods. Change in the protein structure was shown to proceed at DMSO concentration in water greater than 60% and result in an increase of the protein helicity. However, this structural state of lysozyme is similar to that of the unstructured peptides obtained by its complete proteolysis and is characterized by parameters of accessibility to solvent and mobility of their intrinsic chromophores. The data obtained evidenced that long range interactions have a little influence on the maintenance of the residual secondary structure of lysozyme in the presence of DMSO.
authors.forename: M D
authors.initials: MD
authors.lastname: Kirkitadze
authors.forename: A K
authors.initials: AK
authors.lastname: Surin
authors.forename: S A
authors.initials: SA
authors.lastname: Potekhin
mesh_terms: D002942:Circular Dichroism; D004121:Dimethyl Sulfoxide / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence
chemical_list: D009113:Muramidase; D004121:Dimethyl Sulfoxide
vernacular_title: Denaturirovannoe sostoianie lizotsima v dimetilsul'fokside.