Structure prediction of proteins--where are we now?
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.
Rost
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B
European Molecular Biology Laboratory, Heidelberg, Germany.
Sander
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C
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