How good are predictions of protein secondary structure?

Kabsch, Wolfgang; Sander, Christian

doi:10.1016/0014-5793(82)80597-8

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How good are predictions of protein secondary structure?

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Kabsch, Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0014579382805978/pdf?md5=0776aae97b64e73d6d2fb791d5342858&pid=1-s2.0-0014579382805978-main.pdf
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Citation

Kabsch, W., & Sander, C. (1983). How good are predictions of protein secondary structure? FEBS Letters, 155(2), 179-182. doi:10.1016/0014-5793(82)80597-8.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-B00E-5

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.