Figure 2 | Scientific Reports

Figure 2

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

Figure 2

Dynamics of glycosylated IgG1 and IgG4 molecules generated using the AlphaFold predicted structures showing differential dynamics of the Fab arms. Data for the presented analysis were generated from 1000 ns implicit solvent simulations. (a) Comparison of antibody conformations at 0, 500, and 1000 ns showing large relaxation dynamics in the Fab domains for both IgG1 and IgG4 molecules. The arrows are a guide to the eye to mark the predominant directions of motion. (b) An illustration of the six-bead model used to quantify interdomain dynamics, with the antibody domains associated with each of the beads marked. (c–e) Probability densities of Fc–Fab distances (\({R}_{23}\) and \({R}_{25}\)), Fc–Fab angles (\({\theta }_{123}\) and \({\theta }_{125}\)), and Fc–Fab dihedral angles (\({\Theta }_{1234}\) and \({\Theta }_{1256}\)). Data for IgG1 and IgG4 molecules are shown in the left and right panels, respectively.

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