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Models of δ‐hemolysin membrane channels and crystal structures
Author(s) -
Raghunathan G.,
Seetharamulu P.,
Brooks B. R.,
Guy H. R.
Publication year - 1990
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340080304
Subject(s) - antiparallel (mathematics) , membrane , hemolysin , crystallography , raft , melittin , crystal (programming language) , materials science , chemistry , chemical physics , physics , copolymer , biochemistry , composite material , programming language , quantum mechanics , virulence , magnetic field , gene , polymer , computer science
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.