Computer simulation of globules with microstructure.

We present recent data of our Monte Carlo computer simulation study of properties of AB-copolymer globules which depend strongly on the primary sequence of A and B monomeric units. Different primary sequences have been studied: random, random-block, regular and designed ones by using some particular spatial conformation of a homopolymer chain (we have compared here three models: protein-like copolymers, AB-copolymers modeling membrane proteins and ABC-copolymers modeling proteins with active enzymatic center). We have found several evidences for the fact that an AB-copolymer chain with a primary sequence prepared on the basis of a particular conformation of a homopolymer chain by some "coloring" procedure preserves the "memory" about its "parent" spatial conformation. Analyzing the power spectra of AB-sequences, we find the existence of long-range power-law correlations for the copolymers with specially designed primary sequences.