Fig. 1

Effects of 2D NMs on protein stability. A Represent active intermediate structures during the inserting processes for all three replicas of independent trajectories, noted as traj1, traj2, and traj3. Dimer-I and dimer-II, taken from different strands, are colored with blue and green, respectively. B Time evolution of heavy atom contact number between two actin dimers. (Reproduced with permission from Ref. [⁹⁴], Copyright 2016, John Wiley and Sons). C Initial and final snapshots of the double-point mutated protein GB1 on graphene from an example simulation. D Distribution of "planar" side-chain residues (left) and lysines (right) in β-sheet regions of protein GB1 that determines the adsorbed orientation of the protein GB1 mutant. E Heat map plot of possible orientation angle regions deduced using the SFG and ATR-FTIR measurements. Pink dots are the obtained orientations from the final 5 ns of MD simulation. F The averaged orientation (θ = 14°, ψ = 8°) of protein GB1 on graphene surface from the final 5 ns of simulation. (Reproduced with permission from Ref. [⁹⁵], Copyright 2019, American Chemical Society)