The Properties of Glycophorin a Transmembrane Helices in Erythrocyte Asymmetric Membrane: A Molecular Dynamics Study
Year: 2011
Author: Paruyr K. Hakobyan, Armen H. Poghosyan, Aram A. Shahinyan
Journal of Atomic and Molecular Sciences, Vol. 2 (2011), Iss. 4 : pp. 281–288
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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Journal Article Details
Publisher Name: Global Science Press
Language: English
DOI: https://doi.org/10.4208/jams.012711.021511a
Journal of Atomic and Molecular Sciences, Vol. 2 (2011), Iss. 4 : pp. 281–288
Published online: 2011-01
AMS Subject Headings: Global Science Press
Copyright: COPYRIGHT: © Global Science Press
Pages: 8
Keywords: Glycophorin A (GpA) protein erythrocyte membrane molecular dynamics simulation helix-helix association.