title: PHD--an automatic mail server for protein secondary structure prediction.
abstract: By the middle of 1993, > 30,000 protein sequences has been listed. For 1000 of these, the three-dimensional (tertiary) structure has been experimentally solved. Another 7000 can be modelled by homology. For the remaining 21,000 sequences, secondary structure prediction provides a rough estimate of structural features. Predictions in three states range between 35% (random) and 88% (homology modelling) overall accuracy. Using information about evolutionary conservation as contained in multiple sequence alignments, the secondary structure of 4700 protein sequences was predicted by the automatic e-mail server PHD. For proteins with at least one known homologue, the method has an expected overall three-state accuracy of 71.4% for proteins with at least one known homologue (evaluated on 126 unique protein chains).
authors.forename: B
authors.initials: B
authors.lastname: Rost
authors.forename: C
authors.initials: C
authors.lastname: Sander
authors.forename: R
authors.initials: R
authors.lastname: Schneider
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D005075:Biological Evolution; D003195:Computer Communication Networks; D016208:Databases, Factual; D008969:Molecular Sequence Data; D016571:Neural Networks, Computer; D009816:Office Automation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment / Q000379:methods*
chemical_list: D011506:Proteins