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Botulinum toxin type A is known to block neuromuscular transmission by binding to acceptor sites on motor or sympathetic nerve terminals, entering the nerve terminals and inhibiting the release of acetylcholine.
We estimated H-bond interaction energies of the putative donor and acceptor sites on the natural AR ligand, DHT, and selected nonsteroidal analogues using the PM3 method to compute the energies of interaction with a single water molecule at each site; PM3 fully optimized conformations of the water-bound species were computed for this purpose.
Dalfopristin is an olefinic macrolactone that binds to the 50S subunit of the prokaryotic ribosome and interferes with the function of peptidyl transferase, thereby inactivating the donor and acceptor sites of the ribosome.