[Partially unfolded state of lysozyme with a developed secondary structure in dimethylsulfoxide].
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.
Timchenko
A A
AA
Kirkitadze
M D
MD
Prokhorov
D A
DA
Potekhin
S A
SA
Serdiuk
I N
IN
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
D009113:Muramidase; D004121:Dimethyl Sulfoxide
Chastichno razvernutoe sostoianie lizotsima s razvitoĭ vtorichnoĭ strukturoĭ v dimetilsul'fokside.