Lysozyme was used to analyse the possibilities of the method of magnetic relaxation for investigating the microstructure of the water-protein layer of spin-labelled preparations of proteins and enzymes. It is shown that the effective correlation time of the dipole-dipole interaction of the spin label-water proton complex (τc) and also the thermodynamic parameters Eeff and ΔSeff reflect the local state of the solvate surroundings of lysozyme in the case of labels with long tails. The presence of conformational transitions of lysozyme is demonstrated with change in temperatures (5-80 °C) and as a result of the attachment of the specific inhibitor NAG. It is concluded that the local physical-chemical properties of the water-protein matrix of spin-labelled lysozyme preparations depend on the conformational state of the protein.
|Number of pages||6|
|Journal||Biophysics (Russian Federation)|
|State||Published - 1 Dec 1977|