Computer simulation study of synthetic 4-helix bundle that binds halothane.
1. The synthetic peptide H10A24 self-assembles in aqueous solution into a 4-helix bundle, which exhibits saturable binding of halothane. 2. Molecular dynamics simulation techniques have been used to study the vacuum structure of this bundle. 3. The simulation, initiated as four ideal parallel alpha-helices, resulted in a compact bundle, whose secondary structure remains predominantly alpha-helical. 4. The hydrophobic core has no apparent pocket large enough to accomodate halothane.
Center for Molecular Modeling, Department of Chemistry, University of Pennsylvania, Philadelphia 19104-6323, USA.
A B
AB
Woska
M L
ML
Klein
D
D
Scharf
D000465:Algorithms; D018685:Anesthetics, Inhalation / Q000737:chemistry*; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003198:Computer Simulation; D006221:Halothane / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011955:Receptors, Drug / Q000737:chemistry*
D018685:Anesthetics, Inhalation; D011506:Proteins; D011955:Receptors, Drug; D006221:Halothane