title: How good are predictions of protein secondary structure?
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.
mesh_terms: D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D011336:Probability; D011487:Protein Conformation