Binding of the volatile general anesthetics halothane and isoflurane to a mammalian beta-barrel protein.
A molecular understanding of volatile anesthetic mechanisms of action will require structural descriptions of anesthetic–protein complexes. Porcine odorant binding protein is a 157 residue member of the lipocalin family that features a large β-barrel internal cavity (515 ± 30 Å3) lined predominantly by aromatic and aliphatic residues. Halothane binding to the β-barrel cavity was determined using f