title: Structure prediction of proteins--where are we now?
abstract: Although the 'structure from sequence' prediction problem remains fundamentally unsolved, new and promising methods in one, two and three dimensions have reopened the field. Significantly improved one-dimensional prediction of secondary structure from multiple sequence alignments is now in routine use. In the two-dimensional approach, inter-residue contacts can be detected by analysis of correlated mutations, albeit with low accuracy. Finally, three-dimensional methods, in which pseudopotentials or information values are derived from the databases, are proving their value for distinguishing between correct and incorrect models.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Rost
authors.forename: C
authors.initials: C
authors.lastname: Sander
mesh_terms: D000595:Amino Acid Sequence; D001671:Biochemistry / Q000639:trends; D003198:Computer Simulation; D016208:Databases, Factual; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment / Q000379:methods