Abstract
By the middle of 1993, >30 000 protein sequences had 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 (e on 126 unique protein chains).
| Original language | English |
|---|---|
| Pages (from-to) | 53-60 |
| Number of pages | 8 |
| Journal | Bioinformatics |
| Volume | 10 |
| Issue number | 1 |
| DOIs | |
| State | Published - Feb 1994 |
| Externally published | Yes |