Figure 1 | Scientific Reports

Figure 1

From: The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions

Figure 1

Free energy landscape of HPV-16 E7 representing the monomer-dimer equilibrium. The free energy landscape from the RAM ensemble is plotted as a function of the radius of gyration of the dimeric system (x-axis) and the number of 3-residue segments with antiparallel β-strand content in the disordered E7N domain of monomer 1 (y-axis). Representative conformations of E7 are shown in light blue; in the dimer state, the second monomer is shown in green. The antiparallel β-strand content in the disordered E7N domain is generally low and mainly comprises of short β-bridges of less than 3 residues in length. Radius of gyration values above 4.3 nm stem from the dissociation of the dimer into two monomers and represent various conformations of the isolated monomers. Representative states of both the monomer and the dimer are associated with different regions of the free energy landscape.

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