File S1 - Hydrophobic Collapse of Trigger Factor Monomer in Solution

The file is divided into three sections: Structural dynamics of TF; Comparisons with NMR study; and GROMOS simulations. The first section illustrates structural deviations of trigger factor in solution, including those of individual domains, in all trajectories. The second section qualitatively compares our results to the NMR study conducted by Yao et al. [30]. The third section shows and discusses the results of 250 ns long simulations run with GROMOS43a1 parameters. Figure S1: Structural dynamics of Trigger factor in solution. Figure S2: Structural deviations of respective domains over time with respect to their conformations in crystal structure. Figure S3: Conservation of -sheet structure between residues K127I129 and T418T422. Figure S4: Results from 250 ns long MD simulations run with GROMOS43a1 forcefield parameters. (PDF)