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 language | English |
|---|---|
| Pages (from-to) | 2836-2840 |
| Journal | Soft Matter |
| Volume | 5 |
| Issue number | 15 |
| DOIs | |
| Publication status | Published - 2009 |
Keywords
- consistent-field theory
- terminal tail domain
- intermediate-filaments
- ionic-strength
- nf-m
- phosphorylation
- conformation
- networks
- subunit
- disease
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