Fig. 5
From: Rinmaker: a fast, versatile and reliable tool to determine residue interaction networks in proteins
Free energy landscape of Trp-Cage as a function of the radius of gyration and of the betweenness centrality at temperatures (left) T = 330 K and (right) T = 480 K. Snapshots of the conformation corresponding to stable local minima are given in A for T = 330 K and in B for T = 480 K with highlighted the Gly11, Arg16 and Tpr6 residues involved in the transition between one minimum to the other. In B it is also possible to observe the denaturated \(\alpha\)-helix highlighted in yellow