Abstract

Packing density and other properties of the microenvironment of tryptophan residues in hen egg-white lysozyme macromolecule have been studied on the basis of the known 3D structure of this protein. Results presented here suggest that the efficiency of action of the group which, in principal, can affect tryptophan fluor<;scence depends not only on the distance between this group and the indole ring, but to a great extent upon the location of this group relative to the indole ring.