Evidence map›Paper›PMID 26098304›Full record

ArticleScientific reports2015

Improving prediction of secondary structure, local backbone angles, and solvent accessible surface area of proteins by iterative deep learning.

Rhys Heffernan, Kuldip Paliwal, James Lyons, Abdollah Dehzangi, Alok Sharma, Jihua Wang, Abdul Sattar, Yuedong Yang, Yaoqi Zhou

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
21.1field-weighted citation impact, top 1% of its field
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

117 citing papers in PubMed, 364 citations in OpenAlex.

  1. Review
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  3. Sequence-Based Prediction for Protein Solvent Accessibility.International journal of molecular sciences · 2025
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  18. Explainable Deep Hypergraph Learning Modeling the Peptide Secondary Structure Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
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  20. Article

57 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 2 countries.

Rhys HeffernanSignal Processing Laboratory, School of Engineering, Griffith University, Brisbane, Australia.
Kuldip PaliwalSignal Processing Laboratory, School of Engineering, Griffith University, Brisbane, Australia.
James LyonsSignal Processing Laboratory, School of Engineering, Griffith University, Brisbane, Australia.
Abdollah Dehzangi1] Signal Processing Laboratory, School of Engineering, Griffith University, Brisbane, Australia [2] Institute for Integrated and Intelligent Systems, Griffith University, Brisbane, Australia.
Alok Sharma1] Institute for Integrated and Intelligent Systems, Griffith University, Brisbane, Australia [2] School of Engineering and Physics, University of the South Pacific, Private Mail Bag, Laucala Campus, Suva, Fiji.
Jihua WangShandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou University, Dezhou, Shandong, China.
Abdul Sattar1] Institute for Integrated and Intelligent Systems, Griffith University, Brisbane, Australia [2] National ICT Australia (NICTA), Brisbane, Australia.
Yuedong YangInstitute for Glycomics and School of Information and Communication Technique, Griffith University, Parklands Dr. Southport, QLD 4222, Australia.
Yaoqi Zhou1] Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou University, Dezhou, Shandong, China [2] Institute for Glycomics and School of Information and Communication Technique, Griffith University, Parklands Dr. Southport, QLD 4222, Australia.
Griffith University · AUDezhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Direct prediction of protein structure from sequence is a challenging problem. An effective approach is to break it up into independent sub-problems. These sub-problems such as prediction of protein secondary structure can then be solved independently. In a previous study, we found that an iterative use of predicted secondary structure and backbone torsion angles can further improve secondary structure and torsion angle prediction. In this study, we expand the iterative features to include solvent accessible surface area and backbone angles and dihedrals based on Cα atoms. By using a deep learning neural network in three iterations, we achieved 82% accuracy for secondary structure prediction, 0.76 for the correlation coefficient between predicted and actual solvent accessible surface area, 19° and 30° for mean absolute errors of backbone φ and ψ angles, respectively, and 8° and 32° for mean absolute errors of Cα-based θ and τ angles, respectively, for an independent test dataset of 1199 proteins. The accuracy of the method is slightly lower for 72 CASP 11 targets but much higher than those of model structures from current state-of-the-art techniques. This suggests the potentially beneficial use of these predicted properties for model assessment and ranking.

Indexed as

Machine LearningAlgorithmsAmino AcidsDatabases, ProteinModels, MolecularProteinsProtein Structure, SecondarySolventsAmino AcidsProteinsSolvents

Identifiers

PMID26098304
PMCPMC4476419
OpenAlexW1596947964

What OpenQuestion holds

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LicenceCC BY
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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.