Summary

Lysozyme adsorption complexes with graphene oxide (GO) and diminished GO have been studied via radiotracer technique utilizing tritium as a label. The experiment contains adsorption examine, with quantity and enzymatic exercise management, and revealing structural peculiarities of lysozyme adsorbed on graphene oxide floor by evaluation of tritium distribution within the amino acid residues after the bombardment with atomic tritium. Experimental and molecular docking outcomes prompt that lysozyme adsorbs immediately on GO by formation of bonds between GO floor and Cys6 and Arg128 that contribute to formation conformation, through which fragrant residues varieties π-π bonds with GO floor, and positively charged amino acid residues bind with O-containing teams of GO by way of electrostatic attraction. Within the follow-up layers lysozyme molecules work together with one another that lead to adjustments and adsorbed lysozyme molecules leading to adjustments in protein construction. Such adjustments are usually not critically important however result in enhance of availability of an energetic web site of the enzyme for binding with a substrate after the desorption from the multilayer.