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- W2076990003 abstract "We demonstrate that cyano-phenylalanine (PheCN) can be utilized to probe the binding of the inhalational anesthetic halothane to a model ion channel protein hbAP-PheCN possessing a designed binding cavity. The Trp to PheCN mutation adjacent the cavity alters neither the α-helical conformation nor the 4-helix bundle structure. The halothane binding properties of hbAP-PheCN, based on fluorescence quenching, are consistent with those of the Trp-prototype, hbAP1. The dependence of fluorescence lifetime on halothane concentration implies a one-dimensional diffusion of halothane along the nonpolar core of the protein bundle." @default.
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- W2076990003 date "2009-02-01" @default.
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- W2076990003 title "Mechanism Of Interaction Between The Volatile Anesthetic Halothane And A Model Ion Channel Protein: Fluorescence And Infrared Spectroscopy Employing A Cyano-phenylalanine Probe And Molecular Dynamics Simulation" @default.
- W2076990003 doi "https://doi.org/10.1016/j.bpj.2008.12.2964" @default.
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