Protein Folding Characterization via Persistent Homology

We use persistent homology to analyze predictions of protein folding by trying to identify global geometric structures that contribute to the error when the protein is misfolded. The goal is to find correlations between global geometric structures, as measured by persistent homology, and the failure to predict the correct folding. This technique could be useful in guiding the energy minimization techniques to the correct minimum corresponding to the desired folding.