As part of Folding@home, you know that proteins change their structures (e.g. transitioning from unfolded to folded conformations). Once a protein is folded, it is very common to think of it as adopting a single structure though. To be fair, this is largely because scientists are reasonably good at solving a single, representative structure of a protein but its much harder to assess what sort of structural changes it undergoes with the same resolution.
In a recent paper from my lab, we set out to quantify how much structural heterogeneity there is in folded proteins (here). We examined a set of proteins ranging from small proteins often used to study protein folding to much larger proteins that are more representative of what is typical in the cell. We found that there is substantial heterogeneity in every case and demonstrated that our results are consistent with existing experimental data. Our ability to capture this heterogeneity should be a powerful advantage given the myriad of ways it can affect a protein’s function.