
doi: 10.1002/prot.20717
pmid: 16187342
Assessment of structure predictions in CASP6 was based on single domains isolated from experimentally determined structures, which were categorized into comparative modeling, fold recognition, and new fold targets. Domain definitions were defined upon visual examination of the structures with the aid of automated domain-parsing programs. Domain categorization was determined by comparison of the target structures with those in the Protein Data Bank at the time each target expired and a variety of sequence and structure-based methods to determine potential homologous relationships.
Models, Molecular, Proteomics, Protein Folding, Sequence Homology, Amino Acid, Molecular Sequence Data, Computational Biology, Proteins, Protein Structure, Secondary, Protein Structure, Tertiary, Animals, Humans, Amino Acid Sequence, Databases, Protein
Models, Molecular, Proteomics, Protein Folding, Sequence Homology, Amino Acid, Molecular Sequence Data, Computational Biology, Proteins, Protein Structure, Secondary, Protein Structure, Tertiary, Animals, Humans, Amino Acid Sequence, Databases, Protein
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