Evidence map›Paper›PMID 21702492›Full record

ArticleJournal of chemical information and modeling2011

Sampling multiple scoring functions can improve protein loop structure prediction accuracy.

Yaohang Li, Ionel Rata, Eric Jakobsson

Abstract read
In one paragraph

Article in Journal of chemical information and modeling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Conformational sampling in template-free protein loop structure modeling: an overview.Computational and structural biotechnology journal · 2013
    Review
  7. Structure prediction of loops with fixed and flexible stems.The journal of physical chemistry. B · 2012
    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

3 authors.

Yaohang LiDepartment of Computer Science, Old Dominion University, Norfolk, Virginia, USA. yaohang@cs.odu.edu
Ionel Rata
Eric Jakobsson

Funding

NATIONAL CENTER FOR DESIGN:BIOMIMETIC NANOCONDUCTOR(RMI)PN2EY016570 · NEI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI JAKOBSSON, ERIC G · 2005 to 2009
$6.6M
Mechanical Force and Neural RegenerationR01NS063405 · NINDS · UNIVERSITY OF MIAMI CORAL GABLES · PI CHIBA, AKIRA, JAKOBSSON, ERIC G · 2008 to 2011
$1.2M
NEI NIH HHS 5PN2EY016570-06NEI NIH HHS PN2 EY016570NINDS NIH HHS 5R01NS063405-02NINDS NIH HHS R01 NS063405
6 · The paper itself

Abstract

Accurately predicting loop structures is important for understanding functions of many proteins. In order to obtain loop models with high accuracy, efficiently sampling the loop conformation space to discover reasonable structures is a critical step. In loop conformation sampling, coarse-grain energy (scoring) functions coupling with reduced protein representations are often used to reduce the number of degrees of freedom as well as sampling computational time. However, due to implicitly considering many factors by reduced representations, the coarse-grain scoring functions may have potential insensitivity and inaccuracy, which can mislead the sampling process and consequently ignore important loop conformations. In this paper, we present a new computational sampling approach to obtain reasonable loop backbone models, so-called the Pareto optimal sampling (POS) method. The rationale of the POS method is to sample the function space of multiple, carefully selected scoring functions to discover an ensemble of diversified structures yielding Pareto optimality to all sampled conformations. The POS method can efficiently tolerate insensitivity and inaccuracy in individual scoring functions and thereby lead to significant accuracy improvement in loop structure prediction. We apply the POS method to a set of 4-12-residue loop targets using a function space composed of backbone-only Rosetta and distance-scale finite ideal-gas reference (DFIRE) and a triplet backbone dihedral potential developed in our lab. Our computational results show that in 501 out of 502 targets, the model sets generated by POS contain structure models are within subangstrom resolution. Moreover, the top-ranked models have a root mean square deviation (rmsd) less than 1 A in 96.8, 84.1, and 72.2% of the short (4-6 residues), medium (7-9 residues), and long (10-12 residues) targets, respectively, when the all-atom models are generated by local optimization from the backbone models and are ranked by our recently developed Pareto optimal consensus (POC) method. Similar sampling effectiveness can also be found in a set of 13-residue loop targets.

Indexed as

Computer SimulationModels, MolecularAmino Acid MotifsProteinsProteins

Identifiers

PMID21702492
PMCPMC3211142

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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.