Evidence map›Paper›PMID 19530247›Full record

ArticleProtein science : a publication of the Protein Society2009

Effective knowledge-based potentials.

Evandro Ferrada, Francisco Melo

Abstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein flexibility in the light of structural alphabets.Frontiers in molecular biosciences · 2015
    Review
  6. Article
  7. Article
  8. Review
  9. The Protein-DNA Interface database.BMC bioinformatics · 2010
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Evandro FerradaDepartamento de Genética Molecular y Microbiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Alameda 340, Santiago, Chile.
Francisco Melo

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Empirical ResearchModels, ChemicalAlgorithmsDisulfidesHydrogen BondingHydrophobic and Hydrophilic InteractionsKnowledgeModels, MolecularProtein ConformationProteinsROC CurveThermodynamicsDisulfidesProteins

Identifiers

PMID19530247
PMCPMC2775215

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.