Effect of Lithium Drug on Binding Affinities of Glycogen Synthase Kinase-3 β to Its Network Partners: A New Computational Approach

The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.jcim.1c00952.

• Figure S1, sampled temperature and potential; Figure S2, sampling period for each temperature bin in AT-MD simulations; Figure S3, structural descriptors along the AT-MD simulation time line; Figure S4, RMSD along the AT-MD simulation time line; Figure S5, effects of ions on structural fluctuations of the protein; Figure S6, changes in secondary structures over AT-MD simulation; Figure S7, system-dependent and protein-dependent metrics for different segments of AT-MD simulations in the presence of NaCl; Figure S8, system-dependent and protein-dependent metrics computed for different segments of AT-MD simulations in the presence of LiCl; Figures S9 and S10, trajectories of affinity values; Figure S11, effect of LiCl on the affinity of GSK-3β to its partners; Table S1, comparison of GSK-3β secondary structures in the presence of sodium and lithium ions; Table S2, comparison of GSK-3β affinities toward its partners in the presence of sodium and lithium ions in the three sets of AT-MD data; Table S3, comparison of z-score values in different segments of MD simulations for set 1 data series; and Table S4, number of GSK-3β PBPs with lower, equal, and higher affinities in the presence of LiCl than those in the presence of NaCl in each pathway (PDF)

• Movies S1a, S1b. Dynamics of GSK-3β in the presence of LiCl (AVI) (AVI)

• Movies S2a, S2b. Dynamics of GSK-3β in the presence of NaCl (AVI) (AVI)