How good are predictions of protein secondary structure?
- 8 May 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 155 (2) , 179-182
- https://doi.org/10.1016/0014-5793(82)80597-8
Abstract
The three most widely used methods for the prediction of protein secondary structure from the amino acid sequence are tested on 62 proteins of known structure using a program package and data collection not previously available. None of these methods predicts better than 56% of the residues correctly, for a three state model (helix, sheet and loop). The algorithms of Robson [J. Mol. Biol. (1978) 120, 97–120] and Lim [J. Mol. Biol. (1974) 88, 873–894] are the best of those tested. New methods, now under development, can be tested against this benchmark.Keywords
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