Corresponding Functional Dynamics across the Hsp90 Chaperone Family: Insights from a Multiscale Analysis of MD Simulations
Figure 6
Fitting of the meta-trajectory with only rigid-body movements.
Two orthogonal views of the template protomer used to fit all configurations of the Grp94, Hsp90 and HtpG meta-trajectory using only rigid-body movements of the two-terminal quasi rigid domains (black for N-term and red for C-term) respect to the middle (blue) one. The protomer is 525 amino acids long and is the structure closest to the average configuration of the full meta-trajectory. The optimal rotation axes are shown as cyan cylinders. The position and orientation of these axes are identified with an iterative procedure to allow the N-term and the C-term domains to perform those movements which best fit, on average, all frames in the meta-trajectory (see also Figure 7 for further details). It is worth noting that the axes are not forced a priori to pass through one of the two boundary residues at the interface between two domains.