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pubmed-article:10089198pubmed:abstractTextA method for recognizing the three-dimensional fold from the protein amino acid sequence based on a combination of hidden Markov models (HMMs) and secondary structure prediction was recently developed for proteins in the Mainly-Alpha structural class. Here, this methodology is extended to Mainly-Beta and Alpha-Beta class proteins. Compared to other fold recognition methods based on HMMs, this approach is novel in that only secondary structure information is used. Each HMM is trained from known secondary structure sequences of proteins having a similar fold. Secondary structure prediction is performed for the amino acid sequence of a query protein. The predicted fold of a query protein is the fold described by the model fitting the predicted sequence the best.lld:pubmed
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pubmed-article:10089198pubmed:dateRevised2000-12-18lld:pubmed
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pubmed-article:10089198pubmed:year1999lld:pubmed
pubmed-article:10089198pubmed:articleTitleFORESST: fold recognition from secondary structure predictions of proteins.lld:pubmed
pubmed-article:10089198pubmed:affiliationAnalytical Biostatistics Section, Mathematical and Statistical Computing Laboratory, The Institute, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892-5626, USA.lld:pubmed
pubmed-article:10089198pubmed:publicationTypeJournal Articlelld:pubmed
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