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Báo cáo khoa học: Binding of the volatile general anesthetics halothane and isoflurane to a mammalian b-barrel protein
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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 b-barrel internal cavity (515 ± 30 A ˚ 3 ) lined predomin-antly by aromatic and aliphatic residues. Halothane binding to theb-barrel cavity was determined using fluorescence quenching of Trp16, and a com-petitive binding assay with 1-aminoanthracene. In addition, the binding of halothane and isoflurane were characterized thermodynamically using iso-thermal titration calorimetry....
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