Structural analysis of antigenic variation and adaptive evolution of the H5N1 neuraminidase gene
Fig 10
Dynamical Cross-Correlation Maps (DCCMs) of wild-type and family-specific position-based mutant NA1 catalytic domains.
The DCCMs for the WT NA1 catalytic domain (specifically, Chain A) and its FSP-based mutant proteins, were derived from 100 ns of molecular dynamics simulation. These maps visualize correlated motions between residue pairs, with red indicating strong positive correlation (residues moving in the same direction) and blue indicating strong negative correlation (residues moving in opposite directions). White and black rectangular boxes highlight regions (e.g., residues 1-40, 140-180, 200-240, 300-380) where the most notable alterations in correlation patterns are observed in the mutants compared to WT. These maps provide atomic-level insights into how FSP mutations perturb the protein’s internal communication networks and conformational flexibility.