We present the results of molecular dynamics simulations of charged proteinlike hydrophobic–hydrophilic (HP) copolymers in a dilute salt-free solution with multivalent counterions under poor solvent conditions. The primary sequence of these copolymers is constructed such that they can self-assemble into a segregated core–shell microstructure thus resembling some of the basic properties of globular proteins. The results are compared with those obtained earlier for the system containing monovalent counterions. The processes of coil-to-globule transition, aggregation of polyions, and counterion condensation are studied in detail as a function of temperature. The main attention is paid to the influence of the counterions of different charge on the aggregation of the copolymers. It is found that multivalent counterions considerably increase the aggregation of the chains, which form in their presence the finite-size aggregates built up from several polyions. However, the striking feature of the aggregation is that this process does not appear to lead to macroscopic phase separation. The mechanism that prevents the phase separation is discussed.