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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