Fold recognition and ab initio structure predictions using Hidden Markov Models and [[beta]]-strand pair potentials..

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Protein structure predictions were submitted for 9 of the target sequences in the competition that ran during 1994. Targets sequences were selected that had no known homology with any sequence of known structure and were members of a reasonably sized family of related but divergent sequences. The objective was either to recognize a compatible fold for the target sequence in the database of known structures or to predict ab initio its rough 3D topology. The main tools used were Hidden Markov models (HMM) for fold recognition, a beta-strand pair potential to predict beta-sheet topology, and the PHD server for secondary structure prediction, Compatible folds were correctly identified in a number of cases and the beta-strand pair potential was shown to be a useful tool for ab initio topology prediction. (C) 1995 Wiley-Liss, Inc.
Publisher
Wiley-Blackwell
Issue Date
1995-11
Language
English
Article Type
Article
Keywords

PROTEIN SECONDARY STRUCTURE; HOMOLOGOUS PROTEINS; ALIGNMENT; DOMAIN

Citation

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.23, no.3, pp.398 - 402

ISSN
0887-3585
DOI
10.1002/prot.340230313
URI
http://hdl.handle.net/10203/72747
Appears in Collection
RIMS Journal Papers
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