[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.e. the water shell should strengthen selectivity of molecular recognition.
Lim
V I
VI
Kliashtornyĭ
V G
VG
D000495:Allosteric Site; D001426:Bacterial Proteins / Q000737:chemistry; D006860:Hydrogen Bonding; D007700:Kinetics; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D009696:Nucleic Acids / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012341:RNA, Ribosomal, 5S / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry; D014867:Water / Q000737:chemistry
D001426:Bacterial Proteins; D009696:Nucleic Acids; D011506:Proteins; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C106696:TL5 protein, Thermus thermophilus; D014867:Water