ArticleJournal of biomolecular NMR2010
Detection of unrealistic molecular environments in protein structures based on expected electron densities.
Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Escaping the cut by restriction enzymes through single-strand self-annealing of host-edited 12-bp and longer synthetic palindromes.DNA and cell biology · 2012Article
- Alternative protein-protein interfaces are frequent exceptions.PLoS computational biology · 2012Article
- Real space refinement of crystal structures with canonical distributions of electrons.Structure (London, England : 1993) · 2011Article
- SHIFTX2: significantly improved protein chemical shift prediction.Journal of biomolecular NMR · 2011Article
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Authors and funding
3 authors.
Funding
Abstract
Understanding the relationship between protein structure and biological function is a central theme in structural biology. Advances are severely hampered by errors in experimentally determined protein structures. Detection and correction of such errors is therefore of utmost importance. Electron densities in molecular structures obey certain rules which depend on the molecular environment. Here we present and discuss a new approach that relates electron densities computed from a structural model to densities expected from prior observations on identical or closely related molecular environments. Strong deviations of computed from expected densities reveal unrealistic molecular structures. Most importantly, structure analysis and error detection are independent of experimental data and hence may be applied to any structural model. The comparison to state-of-the-art methods reveals that our approach is able to identify errors that formerly remained undetected. The new technique, called RefDens, is accessible as a public web service at http://refdens.services.came.sbg.ac.at.
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