TCB Publications - Abstract

Rosemary Braun, Donald M. Engelman, and Klaus Schulten. Molecular dynamics simulations of micelle formation around dimeric glycophorin A transmembrane helices. Biophysical Journal, 87:754-763, 2004. (PMC: 1304485)

BRAU2004 Insertion and formation of membrane proteins involves the interaction of protein helices with one another in lipid environments. Engelman and coworkers have studied glycophorin A (GpA) transmembrane helices embedded in sodium dodecyl sulfate (SDS) micelles in order to identify contacts significant for helix dimerization. However, a detailed picture of the conformation and dynamics of the GpA-SDS system cannot be obtained solely through experiment. Molecular dynamics simulations of SDS and a GpA dimer can provide an atomic-level picture of SDS aggregation and helix association. We report 2.5 ns simulations of GpA wild-type and mutants in a pre-formed micelle as well as a 32 ns simulation showing the formation of a complete micelle around wild- type GpA from an initially random placement of SDS molecules in the aqueous environment. In the latter case, an initial instability of GpA helices in water is reversed after the helices become surrounded by SDS. The properties of the spontaneously formed micelle surrounding the GpA are indistinguishable from those of the pre-formed micelle surrounding the GpA dimer.

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