[Crystal structures of mutant ribosomal proteins L1].

Nine mutant forms of ribosomal proteins L1 from the bacterium Thermus thermophilus and the archaeon Methanococcus jannaschii were obtained. Their crystal structures were determined and analyzed. Earlier determined structure of S179C TthL1 was also thoroughly analyzed.

[Kinetic, energetic and stereochemical factors determining molecular recognition of proteins and nucleic acids].

It is shown within the framework of stereochemical modeling that disruption of water shells of proteins and nucleic acids is confronted by significant kinetic barriers caused by the breaking of hydrogen bonds. The structure of the water shells is dictated by the surface of proteins and nucleic acids, therefore the kinetic barriers due to disruption of the water shell are strongly distinct from each other on different parts of the shell. This, in turn, means that the probability of participation of different parts of the protein and nucleic acid surfaces in intermolecular interactions should be varied through a wide range, i.