Abstract
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.
Original language | English (US) |
---|---|
Pages (from-to) | 140-144 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 578 |
Issue number | 1-2 |
DOIs | |
State | Published - Dec 3 2004 |
Keywords
- Analytical ultracentrifugation
- Anesthesia
- Halothane
- Hydrogen exchange
- Protein cavities
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology