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Article: Binding of the general anesthetics chloroform and 2,2,2-trichloroethanol to the hydrophobic core of a four-alpha-helix bundle protein
- Article from:
- Photochemistry and Photobiology
- Article date:
- January 1, 2003
- Author:
CopyrightCopyright American Society of Photobiology Jan 2003. Provided by ProQuest LLC. (Hide copyright information)
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Binding of the General Anesthetics Chloroform and 2,2,2-Trichloroethanol to the Hydrophobic Core of a Four-alpha-Helix Bundle Protein(para)
ABSTRACT
The structural features of general anesthetic binding sites on proteins are being examined using a defined model system consisting of a four-alpha-helix bundle scaffold with a hydrophobic core. Previous work suggested that halothane binding to the four-alpha-helix bundle was improved by (1) introducing a cavity into the hydrophobic core and (2) substituting a methionine side-chain in place of an alpha-helical heptad e position leucine. In this study, the ability of the general anesthetics chloroform and 2,2,2-trichloroethanol to bind to the ...