Quantitative description of side chain effects on binding to protein.
Values of delta delta G previously reported for transition state binding of ATP and tyrosine by tyrosyl-tRNA synthetase as a function of side chain structure are quantitatively described by the intermolecular force (IMF) equation. Polarizability, ionic side chains, and steric effects seem to be the major factors in determining delta delta G. A contribution from hydrogen bonding cannot be excluded but is at best probably small. Binding is apparently due to dispersion forces and ion/dipole and ion-induced/dipole interactions.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D006860:Hydrogen Bonding; D007700:Kinetics; D008433:Mathematics; D011485:Protein Binding; D013816:Thermodynamics; D014443:Tyrosine / Q000378:metabolism*; D014448:Tyrosine-tRNA Ligase / Q000378:metabolism*
D014443:Tyrosine; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D014448:Tyrosine-tRNA Ligase