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How good are predictions of protein secondary structure?
Author(s) -
Kabsch Wolfgang,
Sander Christian
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80597-8
Subject(s) - protein secondary structure , protein structure prediction , benchmark (surveying) , amino acid residue , sequence (biology) , chemistry , protein structure , peptide sequence , computational biology , computer science , biology , biochemistry , geography , geodesy , gene
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.