Figure 1 | Scientific Reports

Figure 1

From: IgG1 and IgG4 antibodies sample initial structure dependent local conformational states and exhibit non-identical Fab dynamics

Figure 1

(a) Snapshots showing AlphaFold predicted structures of IgG1 and IgG4 antibodies and the corresponding conformations after 1 ns of molecular dynamics relaxation. The positions of cysteine residues forming disulfide bonds are displayed as Van der Waals beads and the spatial location of the hinge regions are marked by circles. (b) Time series of the root mean squared deviation (RMSD) in the alpha carbon (\({C}_{\alpha })\) positions for the whole antibody (all), Fc, Fab1 and Fab2 domains. The individual domains undergo a minor rearrangement and stabilize with 0.1 ns, while the rmsd for the whole antibody shows a growing trend even past 1 ns. (c) Time series showing the number of non-covalent interactions between the Fc, Fab1 and Fab2 domains. Fc–Fab2 interactions are dominant in IgG1 while the Fc interacts with both Fabs in IgG4. Fab1–Fab2 interactions are non-existent in both molecules.

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