Abstract
Newly determined protein structures are classified to belong to a new fold, if the structures are sufficiently dissimilar from all other so far known protein structures. To analyse structural similarities of proteins, structure alignment tools are used. We demon-strate that the usage of non-sequential structure alignment tools, that neglect the polypeptide chain connectivity, can yield structure alignments with significant similarities between proteins of known 3D structure and newly determined protein structures that possess a new fold.

Citation
"Novel protein folds and their non-sequential structural analogues, Guerler, A., Knapp, E.W., Protein Science, 2008 (accepted)"

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