Applying self-consistent field theory, we consider a coarse-grained model for the polymerlike projections of neurofilament (NF) proteins that form a brush structure around neurofilaments. We focus on effects of molecular composition, which is the relative occurrence of NF-H, NF-M, and NF-L proteins, on the organization of NF projection domains. We consider NF brushes with selectively truncated projections, and with a varied ratio L:H:M of constituent tails. Our conclusion is that the NF brush structure is remarkably tolerant with respect to the variation in M and H chains. Results compare favorably with experimental data on model animals, provided that due attention is paid on the level of phosphorylation of the KSP repeats.
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