Evidence map›Paper›PMID 20667087›Full record

ArticleBMC bioinformatics2010

Sequence-based identification of interface residues by an integrative profile combining hydrophobic and evolutionary information.

Peng Chen, Jinyan Li

Abstract read
In one paragraph

Article in BMC bioinformatics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

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15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
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  5. Article
  6. Special Protein Molecules Computational Identification.International journal of molecular sciences · 2018
    Article
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  9. Review
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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Peng ChenBioinformatics Research Center, School of Computer Engineering, Nanyang Technological University, 639798 Singapore.
Jinyan Li

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein-protein interactions play essential roles in protein function determination and drug design. Numerous methods have been proposed to recognize their interaction sites, however, only a small proportion of protein complexes have been successfully resolved due to the high cost. Therefore, it is important to improve the performance for predicting protein interaction sites based on primary sequence alone.

resultsWe propose a new idea to construct an integrative profile for each residue in a protein by combining its hydrophobic and evolutionary information. A support vector machine (SVM) ensemble is then developed, where SVMs train on different pairs of positive (interface sites) and negative (non-interface sites) subsets. The subsets having roughly the same sizes are grouped in the order of accessible surface area change before and after complexation. A self-organizing map (SOM) technique is applied to group similar input vectors to make more accurate the identification of interface residues. An ensemble of ten-SVMs achieves an MCC improvement by around 8% and F1 improvement by around 9% over that of three-SVMs. As expected, SVM ensembles constantly perform better than individual SVMs. In addition, the model by the integrative profiles outperforms that based on the sequence profile or the hydropathy scale alone. As our method uses a small number of features to encode the input vectors, our model is simpler, faster and more accurate than the existing methods.

conclusionsThe integrative profile by combining hydrophobic and evolutionary information contributes most to the protein-protein interaction prediction. Results show that evolutionary context of residue with respect to hydrophobicity makes better the identification of protein interface residues. In addition, the ensemble of SVM classifiers improves the prediction performance. AVAILABILITY: Datasets and software are available at http://mail.ustc.edu.cn/~bigeagle/BMCBioinfo2010/index.htm.

Indexed as

Evolution, MolecularAlgorithmsAmino Acid SequenceHumansHydrophobic and Hydrophilic InteractionsModels, MolecularProteinsSoftwareProteins

Identifiers

PMID20667087
PMCPMC2921408

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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.