Modeling mutations and homologous proteins.
A protein sequence with at lease 40% identity to a known structure can now be modelled automatically, with an accuracy approaching that o fa low-resolution X-ray structure or a medium-resolution nuclear magnetic resonance structure. In general, these models have goods stereochemistry and an overall structural accuracy that is as high as the similarity between the template and the actual structure being predicted. As a result, the number of sequences that can be modelled is an order of magnitude larger then the number of experimentally determined protein structures. In addition, evaluation techniques are available that can estimated errors in different regions of the model. Thus, the number of applications where homology modelling is proving useful is growing rapidly.
Sali
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The Rockefeller University, New York, USA.
D000595:Amino Acid Sequence; D003198:Computer Simulation; D016208:Databases, Factual; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment
D011506:Proteins