Evolutionary similarity among peptide segments is a basis for prediction of protein folding

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Abstract
Short segments of polypeptide, from a protein for which the primary sequence but not the three‐dimensional structure is known, are compared to a library of known structures. The basis of comparison is the probability with which residues in the unknown segment might substitute through evolution for residues in segments of known structure. In test cases, segments from known structures that are similar in sequence to those from a protein treated as unknown are often found to be similar in three‐dimensional structure to one another and to the true structure of the “unknown” segment. This provides a basis for prediction of the local configuration (secondary structure) of polypeptides.