An Unsupervised approach for augmentation of Protein Structure

Among several possible effects of mutations, protein stability is the most critical factor related to protein function. The destabilization of a protein is due to misfolding or the glassy state of a protein which occurs due to the wrong amino acid substit utions. This destabilization is cause of many prion diseases. A check on stability of the protein could be an efficient solution for this problem, in this paper such an unsupervised approach is proposed.