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- W2061888384 abstract "Oligomerization of transmembrane (TM) helices is a key stage in the folding of membrane proteins. Glycophorin A (GpA) is a well-documented test system for this process. Coarse-grained molecular dynamics (CG-MD) allows us to simulate the self-assembly of TM helices into dimers, for both wild-type (WT) and mutant GpA sequences. For the WT sequences, dimers formed rapidly and remained stable in all simulations. The resultant dimers exhibited right-handed crossing and the same interhelix contacts as in NMR structures. Simulations of disruptive mutants revealed the dimers were less stable, with values of ΔΔGdimerization consistent with experimental data. The dimers of disruptive mutants were distorted relative to the WT and showed left-handed crossing of their helices. CG-MD can therefore be used to explore the interactions of TM helices, an important stage in the folding of membrane proteins. In particular, CG-MD has been shown to be sensitive enough to detect disruptions introduced by mutation. Future refinement of such models via atomistic simulations will enable a multiscale approach to predict the folding of membrane proteins." @default.
- W2061888384 created "2016-06-24" @default.
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- W2061888384 creator A5033094392 @default.
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- W2061888384 date "2008-09-11" @default.
- W2061888384 modified "2023-09-23" @default.
- W2061888384 title "Helix−Helix Interactions in Membrane Proteins: Coarse-Grained Simulations of Glycophorin A Helix Dimerization" @default.
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- W2061888384 doi "https://doi.org/10.1021/bi800678t" @default.
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