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Amino acid mutation(s) that cause(s) partial or total unfolding of a protein can lead to disease states and failure to produce mutants. It is therefore very useful to be able to predict which mutations can retain the conformation of a wild-type protein and which mutations will lead to local or global unfolding of the protein. We have developed a fast and reasonably accurate method based on a backbonedependent side-chain rotamer library to predict the (folded or unfolded) conformation of adoi:10.1093/protein/14.7.479 pmid:11522921 fatcat:esbni2kz5bg5balw3qko5w5s5a