PHD-an automatic mail server for protein secondary structure prediction (original) (raw)
Journal Article
,
EMBL, Meyerhofstrasse I, D-69117 Heidelberg, Germany
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EMBL, Meyerhofstrasse I, D-69117 Heidelberg, Germany
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EMBL, Meyerhofstrasse I, D-69117 Heidelberg, Germany
Search for other works by this author on:
Accepted:
30 September 1993
Published:
01 February 1994
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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).
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