The model of protein-like copolymer with hydrogen bonds

The results are presented of Langevin dynamics computer simulation of binary hydrogen bonds influence on protein-like AB-copolymer coil-globule transition. The effect of the distribution of hydrogen bond sites along primary sequence on the formation of globular conformations is studied. It is found that the presence of binary hydrogen bonds stabilizes protein-like globular structure when we increase temperature. The positions of hydrogen bond sites along primary sequence are not very important, as well as the type of monomer unit (A or B) which is associated with given hydrogen bond. The number of binary hydrogen bonds is essential when we estimate temperature stability of protein-like globular structure.