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On the polyelectrolyte brush model of neurofilaments

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Abstract

We use scaling arguments and numerical self-consistent-field theory to highlight the structure of a biological polyelectrolyte (PE) brush formed by projection domains of a triplet neurofilament (NF) protein. The protein chains are coarse-grained on the amino acid level and grouped by their polarity and chargability. In the numerical model the full primary sequence is taken, whereas in the scaling approach sequence-averaged properties are accounted for. We elaborate on the electrostatic regulation of the brush structure and discuss its role in the formation of the NF network inside axons
Original languageEnglish
Pages (from-to)2836-2840
JournalSoft Matter
Volume5
Issue number15
DOIs
Publication statusPublished - 2009

Keywords

  • consistent-field theory
  • terminal tail domain
  • intermediate-filaments
  • ionic-strength
  • nf-m
  • phosphorylation
  • conformation
  • networks
  • subunit
  • disease

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