Prediction of protein loop geometries in solution
| Autor: | Aart J. Nederveen, Gloria Fuentes, Chaya S. Rapp, Temima Strauss |
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| Přispěvatelé: | Amsterdam Cardiovascular Sciences, Amsterdam Neuroscience, Radiology and Nuclear Medicine |
| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Protein Folding Loop (graph theory) Protein Conformation Chemistry Protein Data Bank (RCSB PDB) Computational Biology Proteins Reproducibility of Results Structure validation Biochemistry Protein Structure Secondary Crystallography Protein structure Global distance test Structural biology Structural Biology Computer Simulation Protein folding Databases Protein Biological system Molecular Biology Root-mean-square deviation Algorithms |
| Zdroj: | Proteins, 69(1), 69-74. Wiley-Liss Inc. |
| ISSN: | 0887-3585 |
| DOI: | 10.1002/prot.21503 |
| Popis: | The ability to determine the structure of a protein in solution is a critical tool for structural biology, as proteins in their native state are found in aqueous environments. Using a physical chemistry based prediction protocol, we demonstrate the ability to reproduce protein loop geometries in experimentally derived solution structures. Predictions were run on loops drawn from (1)NMR entries in the Protein Databank (PDB), and from (2) the RECOORD database in which NMR entries from the PDB have been standardized and re-refined in explicit solvent. The predicted structures are validated by comparison with experimental distance restraints, a test of structural quality as defined by the WHAT IF structure validation program, root mean square deviation (RMSD) of the predicted loops to the original structural models, and comparison of precision of the original and predicted ensembles. Results show that for the RECOORD ensembles, the predicted loops are consistent with an average of 95%, 91%, and 87% of experimental restraints for the short, medium and long loops respectively. Prediction accuracy is strongly affected by the quality of the original models, with increases in the percentage of experimental restraints violated of 2% for the short loops, and 9% for both the medium and long loops in the PDB derived ensembles. We anticipate the application of our protocol to theoretical modeling of protein structures, such as fold recognition methods; as well as to experimental determination of protein structures, or segments, for which only sparse NMR restraint data is available. |
| Databáze: | OpenAIRE |
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