[Coil--globule transition in a linear macromolecule]

Effect of chain length and rigidity on characteristics of coil-globule in a linear macromolecule was considered taking into account the data of computer experiment. It was shown that with a temperature decrease a sufficiently long chain passes from a developed conformation into the globule close to theta-point. Relative withdrawal of theta-temperature from that of coil-globule transition is changed in proportion to the persistent length of the chain. The role of intramolecular orientation ordering during the formation of the protein globule is discussed.