Fig. 4: A biophysically relevant network can be derived from the correlation matrix revealing residues playing a central role in interface dynamics.
a The network encoding interface dynamics, where each node (black) represents an interface residue and edges (green) are significant correlations between residues whose alpha-carbon distance does not surpass 10 Å. Edge transparency and width are scaled according to |ρs|. Secondary structure features of the interface have been labelled. b Secondary structure features of the H‑2Db/peptide interface colored according to the same label colors as in a. Various informative network centrality measures can be mapped to structure: c unweighted degree centrality, d betweenness centrality, e closeness centrality, f eigenvector centrality, and g coreness. Plots showing centrality measures per residue are provided (Supplementary Fig 19).
