Volume 2, Issue 4
The properties of glycophorin A transmembrane helices in erythrocyte asymmetric membrane: a molecular dynamics study

Paruyr K. Hakobyan, Armen H. PoghosyanAram A. Shahinyan

J. At. Mol. Sci., 2 (2011), pp. 281-288.

Published online: 2011-02

Preview Full PDF 92 2900
Export citation
  • 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.

  • Keywords

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

  • AMS Subject Headings

  • Copyright

COPYRIGHT: © Global Science Press

  • Email address

paruyr.hakobyangmail.com (Paruyr K. Hakobyan)

  • BibTex
  • RIS
  • TXT
@Article{JAMS-2-281, author = {Hakobyan , Paruyr K. and Poghosyan , Armen H. and Shahinyan , Aram A.}, title = {The properties of glycophorin A transmembrane helices in erythrocyte asymmetric membrane: a molecular dynamics study}, journal = {Journal of Atomic and Molecular Sciences}, year = {2011}, volume = {2}, number = {4}, pages = {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.}, issn = {2079-7346}, doi = {https://doi.org/10.4208/jams.012711.021511a}, url = {http://global-sci.org/intro/article_detail/jams/8162.html} }
TY - JOUR T1 - The properties of glycophorin A transmembrane helices in erythrocyte asymmetric membrane: a molecular dynamics study AU - Hakobyan , Paruyr K. AU - Poghosyan , Armen H. AU - Shahinyan , Aram A. JO - Journal of Atomic and Molecular Sciences VL - 4 SP - 281 EP - 288 PY - 2011 DA - 2011/02 SN - 2 DO - http://doi.org/10.4208/jams.012711.021511a UR - https://global-sci.org/intro/article_detail/jams/8162.html KW - Glycophorin A (GpA) protein KW - erythrocyte membrane KW - molecular dynamics simulation KW - helix-helix association AB - 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.
Paruyr K. Hakobyan , Armen H. Poghosyan & Aram A. Shahinyan . (2019). The properties of glycophorin A transmembrane helices in erythrocyte asymmetric membrane: a molecular dynamics study. Journal of Atomic and Molecular Sciences. 2 (4). 281-288. doi:10.4208/jams.012711.021511a
Copy to clipboard
The citation has been copied to your clipboard