Abstract
The main characteristics of lysozyme globules in solutions, including the sizes of cores and fringelike surface layers, are determined from the data of calorimetry (lysozyme-denaturation temperatures in solution) and light scattering, via the method of atomic contributions, and from the Flory-Fox equation. It is shown that the enzymatic activity of lysozyme is governed by fringelike surface-layer loops that contain amino acid residues forming the active sites of lysozyme. Methylresorcinol affects the enzymatic activity of lysozyme owing to a change in the properties of fringelike surface layers.
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