Selected article for: "amino acid and transmembrane protein"

Author: Chen, Cheng-Chang; Krüger, Jens; Sramala, Issara; Hsu, Hao-Jen; Henklein, Peter; Chen, Yi-Ming Arthur; Fischer, Wolfgang B.
Title: ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations
  • Cord-id: 7aw17jf8
  • Document date: 2010_8_12
  • ID: 7aw17jf8
    Snippet: 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 p
    Document: 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.

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