ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations

Cheng Chang Chen, Jens Krüger, Issara Sramala, Hao Jen Hsu, Peter Henklein, Yi Ming Arthur Chen, Wolfgang B. Fischer

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9 ± 0.8 pS at elevated temperature (38.5 °C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.

Original languageEnglish
Pages (from-to)572-579
Number of pages8
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1808
Issue number2
DOIs
StatePublished - Feb 2011

Keywords

  • Bilayer recording
  • Ion channel
  • Molecular dynamics
  • ORF8a
  • SARS-CoV

Fingerprint

Dive into the research topics of 'ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations'. Together they form a unique fingerprint.

Cite this