Models of delta-hemolysin membrane channels and crystal structures.

Article Details

Citation

Raghunathan G, Seetharamulu P, Brooks BR, Guy HR

Models of delta-hemolysin membrane channels and crystal structures.

Proteins. 1990;8(3):213-25.

PubMed ID
2281085 [ View in PubMed
]
Abstract

Molecular modeling and energy calculations have been used to study how delta-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 delta-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 delta-hemolysin with six or eight monomers per channel.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Delta-hemolysinP0C1V1Details