The Properties of Glycophorin a Transmembrane Helices in Erythrocyte Asymmetric Membrane: A Molecular Dynamics Study

Authors

  • Paruyr K. Hakobyan International Scientific-Educational Center NAS RA 0019, Yerevan, Armenia
  • Armen H. Poghosyan International Scientific-Educational Center NAS RA 0019, Yerevan, Armenia
  • Aram A. Shahinyan Institute of Applied Problems of Physics NAS RA 0014, Yerevan, Armenia

DOI:

https://doi.org/10.4208/jams.012711.021511a

Keywords:

Glycophorin A (GpA) protein, erythrocyte membrane, molecular dynamics simulation, helix-helix association.

Abstract

We have performed an 80ns molecular dynamics (MD) simulation of human red blood erythrocyte asymmetric membrane model. The NAMD code and CHARMM27 force field were used. We have estimated some features of embedded Glycophorin A (GpA) protein and have discussed some important problems concerning the interaction between the protein and surrounding media. It is stated that the lipid environment and protein immediate neighboring lead to the changes in helix-helix association, as well as to the protein orientation. The interaction nature between protein and neighboring phospholipid chains are dominant forces governing to helix-helix association.

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Published

2011-02-01

Issue

Vol. 2 No. 4 (2011)

Section

Articles