ArticleProtein science : a publication of the Protein Society2009
Effective knowledge-based potentials.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- Atomic-level protein-ligand recognition with PBCNet2.0 for probe discovery.Nature chemical biology · 2026Article
- ANDIS: an atomic angle- and distance-dependent statistical potential for protein structure quality assessment.BMC bioinformatics · 2019Article
- All-Atom Four-Body Knowledge-Based Statistical Potentials to Distinguish Native Protein Structures from Nonnative Folds.BioMed research international · 2017Article
- Principal component analysis of binding energies for single-point mutants of hT2R16 bound to an agonist correlate with experimental mutant cell response.Journal of computational biology : a journal of computational molecular cell biology · 2015Article
- Protein flexibility in the light of structural alphabets.Frontiers in molecular biosciences · 2015Review
- Trends in template/fragment-free protein structure prediction.Theoretical chemistry accounts · 2011Article
- Predicting changes in protein thermostability brought about by single- or multi-site mutations.BMC bioinformatics · 2010Article
- Human allelic variation: perspective from protein function, structure, and evolution.Current opinion in structural biology · 2010Review
- The Protein-DNA Interface database.BMC bioinformatics · 2010Article
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2 authors.
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Abstract
Empirical or knowledge-based potentials have many applications in structural biology such as the prediction of protein structure, protein-protein, and protein-ligand interactions and in the evaluation of stability for mutant proteins, the assessment of errors in experimentally solved structures, and the design of new proteins. Here, we describe a simple procedure to derive and use pairwise distance-dependent potentials that rely on the definition of effective atomic interactions, which attempt to capture interactions that are more likely to be physically relevant. Based on a difficult benchmark test composed of proteins with different secondary structure composition and representing many different folds, we show that the use of effective atomic interactions significantly improves the performance of potentials at discriminating between native and near-native conformations. We also found that, in agreement with previous reports, the potentials derived from the observed effective atomic interactions in native protein structures contain a larger amount of mutual information. A detailed analysis of the effective energy functions shows that atom connectivity effects, which mostly arise when deriving the potential by the incorporation of those indirect atomic interactions occurring beyond the first atomic shell, are clearly filtered out. The shape of the energy functions for direct atomic interactions representing hydrogen bonding and disulfide and salt bridges formation is almost unaffected when effective interactions are taken into account. On the contrary, the shape of the energy functions for indirect atom interactions (i.e., those describing the interaction between two atoms bound to a direct interacting pair) is clearly different when effective interactions are considered. Effective energy functions for indirect interacting atom pairs are not influenced by the shape or the energy minimum observed for the corresponding direct interacting atom pair. Our results suggest that the dependency between the signals in different energy functions is a key aspect that need to be addressed when empirical energy functions are derived and used, and also highlight the importance of additivity assumptions in the use of potential energy functions.
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