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FEBS Lett. 2004 Dec 3;578(1-2):140-4.

Volatile anesthetic modulation of oligomerization equilibria in a hexameric model peptide.

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Department of Biophysics and Biochemistry, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.


To determine if occupancy of interfacial pockets in oligomeric proteins by volatile anesthetic molecules can allosterically regulate oligomerization equilibria, variants of a three-helix bundle peptide able to form higher oligomers were studied with analytical ultracentrifugation, hydrogen exchange and modeling. Halothane shifted the oligomerization equilibria towards the oligomer only in a mutation predicted to create sufficient volume in the hexameric pocket. Other mutations at this residue, predicted to create a too small or too polar pocket, were unaffected by halothane. Inhaled anesthetic modulation of oligomerization interactions is a novel and potentially generalizable biophysical basis for some anesthetic actions.

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