The promoters of cell adhesion are ligands, which are often attached to fle
xible tethers that bind to surface receptors on adjacent cells. Using a com
bination of Monte Carte simulations, diffusion reaction theory, and direct
experiments (surface force measurements) of the biotin-streptavidin system,
we have quantified polymer chain dynamics and the kinetics and spatial ran
ge of tethered ligand-receptor binding. The results show that the efficienc
y of strong binding does not depend solely on the molecular architecture or
binding energy of the receptor-ligand pair, nor on the equilibrium configu
ration of the polymer tether, but rather on its "rare" extended conformatio
ns.