title: Cornering and catching the common protein fold.
abstract: Protein coding regions (genomic DNA) and cDNA sequences can be screened rapidly to help identify them. If a protein's three-dimensional fold can also be identified, then modelling can provide an estimate of the protein's structure, which can assist both in drug design and in probing structure-function relationships. Methods linking one-dimensional information, represented by the sequence, to three-dimensional information of the protein fold are key to this progression of events. The major difficulty lies with the identification of related proteins whose sequences have diverged beyond recognition, while their folds remain similar enough to confirm their descent from a common ancestor.
authors.affiliation: Molecular Modelling and Biocomputing Group, Turku Centre for Biotechnology, Finland. mark.johnson@hops.btk.utu.fi
authors.forename: M S
authors.initials: MS
authors.lastname: Johnson
mesh_terms: D000595:Amino Acid Sequence; D015195:Drug Design; D006454:Hemoglobins / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011487:Protein Conformation; D015202:Protein Engineering; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D006454:Hemoglobins; D011506:Proteins