A hypothesis concerning diffusion-limited protein-ligand interactions.
A simple assumption allows the prediction of the numerical value for a 'universal' limiting kinetic rate for wholly diffusion-limited reactions between small neutral molecules and macromolecules. This prediction is compared with appropriate experimental data for binding of ligands to myoglobin and to enzymes. It is shown that in the absence of electrostatic effects, this limit is approached but not exceeded. The model also makes very specific predictions concerning the viscosity and temperature dependence of such reactions.
van Holde
K E
KE
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331-7305, USA. vanholdk@ucs.orst.edu
D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D014783:Viscosity
D008024:Ligands; D011506:Proteins