Evidence map›Paper›PMID 21244273›Full record

ArticleJournal of computational biology : a journal of computational molecular cell biology2011

Fast geometric consensus approach for protein model quality assessment.

Rafal Adamczak, Jaroslaw Pillardy, Brinda K Vallat, Jaroslaw Meller

Abstract read
In one paragraph

Article in Journal of computational biology : a journal of computational molecular cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

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0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. AlphaFold model quality self-assessment improvement via deep graph learning.Protein science : a publication of the Protein Society · 2025
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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

4 authors.

Rafal AdamczakDepartment of Environmental Health, University of Cincinnati College of Medicine, Cincinnati, Ohio 45226, USA.
Jaroslaw Pillardy
Brinda K Vallat
Jaroslaw Meller

Funding

REPRODUCTIVE AND DEVELOPMENTAL TOXICOLOGY RESEARCHP30ES006096 · NIEHS · UNIVERSITY OF CINCINNATI · PI YADAV, JAGJIT S · 1992 to 2022
$35.4M
Optimization of Stuctures and Networks of ProteinsR01GM067823 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ELBER, RON · 2004 to 2010
$1.9M
NIEHS NIH HHS P30-ES006096NIGMS NIH HHS GM067823PHS HHS A1055649
6 · The paper itself

Abstract

Model quality assessment (MQA) is an integral part of protein structure prediction methods that typically generate multiple candidate models. The challenge lies in ranking and selecting the best models using a variety of physical, knowledge-based, and geometric consensus (GC)-based scoring functions. In particular, 3D-Jury and related GC methods assume that well-predicted (sub-)structures are more likely to occur frequently in a population of candidate models, compared to incorrectly folded fragments. While this approach is very successful in the context of diversified sets of models, identifying similar substructures is computationally expensive since all pairs of models need to be superimposed using MaxSub or related heuristics for structure-to-structure alignment. Here, we consider a fast alternative, in which structural similarity is assessed using 1D profiles, e.g., consisting of relative solvent accessibilities and secondary structures of equivalent amino acid residues in the respective models. We show that the new approach, dubbed 1D-Jury, allows to implicitly compare and rank N models in O(N) time, as opposed to quadratic complexity of 3D-Jury and related clustering-based methods. In addition, 1D-Jury avoids computationally expensive 3D superposition of pairs of models. At the same time, structural similarity scores based on 1D profiles are shown to correlate strongly with those obtained using MaxSub. In terms of the ability to select the best models as top candidates 1D-Jury performs on par with other GC methods. Other potential applications of the new approach, including fast clustering of large numbers of intermediate structures generated by folding simulations, are discussed as well.

Indexed as

Models, MolecularComputational BiologyConsensusDatabases, ProteinProteinsTime FactorsProteins

Identifiers

PMID21244273
PMCPMC3228594

What OpenQuestion holds

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Registered trials

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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.