Evaluation of current techniques for ab initio protein structure prediction.
The results of a protein structure prediction contest are reviewed. Twelve different groups entered predictions on 14 proteins of known sequence whose structures had been determined but not yet disseminated to the scientific community. Thus, these represent true tests of the current state of structure prediction methodologies. From this work, it is clear that accurate tertiary structure prediction is not yet possible. However, protein fold and motif prediction are possible when the motif is recognizable similar to another known structure. Internal symmetry and the information inherent in an aligned family of homologous sequences facilitate predictive efforts. Novel folds remain a major challenge for prediction efforts.
Defay
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Graduate Group in Biophysics, University of California, San Francisco 94131-0450, USA.
Cohen
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D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins; D003196:Computer Graphics; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases; D009682:Magnetic Resonance Spectroscopy; D008562:Membrane Glycoproteins / Q000737:chemistry; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D050857:Synaptotagmins; D001616:beta-Galactosidase / Q000737:chemistry
D002135:Calcium-Binding Proteins; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D011506:Proteins; D050857:Synaptotagmins; D006026:Glycoside Hydrolases; D001616:beta-Galactosidase; C022361:6-phospho-beta-galactosidase