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Protein's residue-wise fluctuation patterns. Monitored Cα-RMSF tones across the whole 100 ns molecular dynamics runs for the investigated hTLR-4 bound epitope vaccine within different oligomeric/saccharide-linked states. (A) glycosylated dimeric, (B) non-glycosylated dimeric, (C) glycosylated monomeric, and (D) non-glycosylated monomeric states, along the sequence residue numbers (bound TLR-4 protein target = 27–627; epitope vaccine = 1–380 residue ranges).
