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How good are predictions of protein secondary structure?

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons93650

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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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0019-B00E-5
Zusammenfassung
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.