MODELS OF DELTA-HEMOLYSIN MEMBRANE CHANNELS AND CRYSTAL-STRUCTURES

Molecular modeling and energy calculations have been used to study how δ‐hemolysin and melittin helices may aggregate on membrane surfaces and insert through membranes to form channels. In these models adjacent antiparallel amphipathic helices form planar “raft” structures, in which one surface is hydrophobic and the other hydrophilic. Models of δ‐hemolysin crystal structure were developed using these “rafts.” These models are based on the unit cell constants and the crystal symmetry obtained from the preliminary crystal data. Energy calculations favor channel models of δ‐hemolysin with six or eight monomers per channel. Copyright © 1990 Wiley‐Liss, Inc.