Protein folds from pair interactions: a blind test in fold recognition

We submitted nine predictions to CASP2 using our fold recognition program ProFIT. Two of these structures were still unsolved by the end of the experiment, six had a recognizable fold, and one fold was new. Four predictions of the six recognizable folds were correct. Two models were excellent in ter...

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Bibliographic Details
Published inProteins, structure, function, and bioinformatics Vol. Suppl 1; pp. 129 - 133
Main Authors Flöckner, H, Domingues, F S, Sippl, M J
Format Journal Article
LanguageEnglish
Published United States 1997
Subjects
Aldose-Ketose Isomerases - chemistry
Amino Acid Sequence
Exfoliatins - chemistry
Fructose-Bisphosphatase - chemistry
Hydro-Lyases - chemistry
Models, Molecular
Molecular Sequence Data
Polyribonucleotide Nucleotidyltransferase - chemistry
Protein Folding
Proteins - chemistry
Threonine Dehydratase - chemistry
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Summary:We submitted nine predictions to CASP2 using our fold recognition program ProFIT. Two of these structures were still unsolved by the end of the experiment, six had a recognizable fold, and one fold was new. Four predictions of the six recognizable folds were correct. Two models were excellent in terms of alignment quality (T0031, T0004): in one the alignment was partially correct (T0014), and one fold was correctly identified (T0038). We discuss improvements of the program and analyze the prediction results.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0887-3585