Ion-dynamics in hepatitis C virus p7 helical transmembrane domains: a molecular dynamics simulation study
Viral proteins assemble into homopolymers in the infected cells and have a role as diffusion-amplifier for ions across subcellular membranes. The homopolymer of hepatitis C virus, protein p7 of strain 1a, which is known to form channels, is used to investigate the dynamics of physiological relevant...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
16 June 2014
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| In: |
Biophysical chemistry
Year: 2014, Volume: 192, Pages: 33-40 |
| ISSN: | 1873-4200 |
| DOI: | 10.1016/j.bpc.2014.06.001 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.bpc.2014.06.001 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0301462214000702 
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| Author Notes: | Yi-Ting Wang, Roman Schilling, Rainer H.A. Fink, Wolfgang B. Fischer |
| Summary: | Viral proteins assemble into homopolymers in the infected cells and have a role as diffusion-amplifier for ions across subcellular membranes. The homopolymer of hepatitis C virus, protein p7 of strain 1a, which is known to form channels, is used to investigate the dynamics of physiological relevant ions, Na+, K+, Cl− and Ca2+ in the vicinity of the protein bundle. The protein bundle is generated by a combination of docking approach and molecular dynamics (MD) simulations. Ion dynamics are recorded during multiple 200ns MD simulations of 1M solutions. His-17 is found to point into the lumen of the pore. Protonation of this residue allows Cl-ions to enter the pore while in its unprotonated state Ca-ions are found within the pore as well. Applied voltage identifies large Cl-ion currents from the site of the loop passing through the pore. Rectification of the current of the Cl-ions is observed. |
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| Item Description: | Gesehen am 03.09.2020 |
| Physical Description: | Online Resource |
| ISSN: | 1873-4200 |
| DOI: | 10.1016/j.bpc.2014.06.001 |