Theoretical Analysis of Structure of Antibody Light Chain Tetramer

In this study, the trajectories of four protomers corresponding to light chain tetramers human antibodies were obtained from MD simulations. The protomers, which should be symmetrically constructed, not completely symmetrical in DSSP analysis and 2D-RMSD showed that although secondary structure is approximately same, deconvolution part α helix leads asymmetry overall simulation. Although number interactions within decreases, between increases, making energy more stable. We hypothesize caused by formation fragment tetramer, hydrogen bonding van der Waals forces lead breakage bond further leading disappearance helix.