Evidence map›Paper›PMID 19958485›Full record

ArticleBMC genomics2009

A modular kernel approach for integrative analysis of protein domain boundaries.

Paul D Yoo, Bing Bing Zhou, Albert Y Zomaya

Abstract read
In one paragraph

Article in BMC genomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
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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

3 authors.

Paul D YooAdvanced Networks Research Group, School of Information Technologies (J12), the University of Sydney, NSW 2006, Australia. dyoo4334@it.usyd.edu.au
Bing Bing Zhou
Albert Y Zomaya

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn this paper, we introduce a novel inter-range interaction integrated approach for protein domain boundary prediction. It involves (1) the design of modular kernel algorithm, which is able to effectively exploit the information of non-local interactions in amino acids, and (2) the development of a novel profile that can provide suitable information to the algorithm. One of the key features of this profiling technique is the use of multiple structural alignments of remote homologues to create an extended sequence profile and combines the structural information with suitable chemical information that plays an important role in protein stability. This profile can capture the sequence characteristics of an entire structural superfamily and extend a range of profiles generated from sequence similarity alone.

resultsOur novel profile that combines homology information with hydrophobicity from SARAH1 scale was successful in providing more structural and chemical information. In addition, the modular approach adopted in our algorithm proved to be effective in capturing information from non-local interactions. Our approach achieved 82.1%, 50.9% and 31.5% accuracies for one-domain, two-domain, and three- and more domain proteins respectively.

conclusionThe experimental results in this study are encouraging, however, more work is need to extend it to a broader range of applications. We are currently developing a novel interactive (human in the loop) profiling that can provide information from more distantly related homology. This approach will further enhance the current study.

Indexed as

Computational BiologyProtein Structure, TertiaryAlgorithmsHumansHydrophobic and Hydrophilic InteractionsProteinsProtein Structure, SecondaryStructural Homology, ProteinProteins

Identifiers

PMID19958485
PMCPMC2788374

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LicenceCC BY
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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.