Effect of rotation on the diffusion-controlled rate of ligand-protein association.
AUTOR(ES)
Hill, T L
RESUMO
The rate of binding a fairly large ligand molecule to a protein is reduced below the usual diffusion-controlled rate by the requirement of a certain rotational orientation. A simple, approximate treatment of this effect is given for special cases of spherical and ellipsoidal ligands. As the center of an ellipsoidal ligand approaches a protein surface, there is an effective repulsive potential between ligand and surface owning to restricted rotation of the ligand. The frequency factor kT/h of the Eyring rate theory is replaced in these reactions involving diffusion in solution by D/Rlambda, where D = diffusion coefficient of ligand, lambda = thermal deBroglie wavelength of ligand, and R = "capture" distance around the binding site on the protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388844Documentos Relacionados
- Diffusion-controlled ligand binding to spheres partially covered by receptors: an effective medium treatment.
- A genetic algorithm for the ligand-protein docking problem
- Experimental study of the diffusion-controlled corrosion of copper in the bottom of a jet stirred reactor
- A three-hybrid system for detecting small ligand–protein receptor interactions
- Experimental resolution of the free energies of aqueous solvation contributions to ligand-protein binding: quinone-QA site interactions in the photosynthetic reaction center protein.