How good are predictions of protein secondary structure?. Kabsch, W & Sander, C FEBS Letters, 155(2):179–182, May, 1983. Paper abstract bibtex 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 et al. [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.
@article{kabsch_how_1983,
title = {How good are predictions of protein secondary structure?},
volume = {155},
url = {http://linkinghub.elsevier.com/retrieve/pii/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 et al. [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.},
language = {eng},
number = {2},
journal = {FEBS Letters},
author = {Kabsch, W and Sander, C},
month = may,
year = {1983},
pmid = {6852232},
pages = {179--182},
}
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