Kinetic, energetic, and stereochemical factors determining the molecular recognition of proteins and nucleic acids

In the context of stereochemical modeling, it has been shown that damage to the hydration shell of proteins and nucleic acids should be confronted by considerable kinetic barriers caused by the breakage of hydrogen bonds of the shell. Since the structure of the hydration shell is determined by the surface of proteins and nucleic acids, the kinetic barriers arising during the breakage of the shell differ greatly in different regions of the biopolymer surface. In turn, this means that the probability of the participation of different surface regions of proteins and nucleic acids in intermolecular interactions should vary within a wide range; i.e., hydration shells should enhance the selectivity of molecular recognition.