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| Title: | PHD - an automatic server for protein secondary structure prediction |
| Author: | Burkhard Rost, Reinhard Schneider & Chris Sander |
| Quote: | CABIOS, 10, 53-60 (1994) |
In the middle of 1993, more than 30,000 protein sequences are known. For 1000 of these the three-dimensional (tertiary) structure is 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 rate between 36% (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).