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Predicting the protein-protein interactions using primary structures with predicted protein surface

BACKGROUND: Many biological functions involve various protein-protein interactions (PPIs). Elucidating such interactions is crucial for understanding general principles of cellular systems. Previous studies have shown the potential of predicting PPIs based on only sequence information. Compared to a...

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Detalles Bibliográficos
Autores principales: Chang, Darby Tien-Hao, Syu, Yu-Tang, Lin, Po-Chang
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3009501/
https://www.ncbi.nlm.nih.gov/pubmed/20122202
http://dx.doi.org/10.1186/1471-2105-11-S1-S3
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author Chang, Darby Tien-Hao
Syu, Yu-Tang
Lin, Po-Chang
author_facet Chang, Darby Tien-Hao
Syu, Yu-Tang
Lin, Po-Chang
author_sort Chang, Darby Tien-Hao
collection PubMed
description BACKGROUND: Many biological functions involve various protein-protein interactions (PPIs). Elucidating such interactions is crucial for understanding general principles of cellular systems. Previous studies have shown the potential of predicting PPIs based on only sequence information. Compared to approaches that require other auxiliary information, these sequence-based approaches can be applied to a broader range of applications. RESULTS: This study presents a novel sequence-based method based on the assumption that protein-protein interactions are more related to amino acids at the surface than those at the core. The present method considers surface information and maintains the advantage of relying on only sequence data by including an accessible surface area (ASA) predictor recently proposed by the authors. This study also reports the experiments conducted to evaluate a) the performance of PPI prediction achieved by including the predicted surface and b) the quality of the predicted surface in comparison with the surface obtained from structures. The experimental results show that surface information helps to predict interacting protein pairs. Furthermore, the prediction performance achieved by using the surface estimated with the ASA predictor is close to that using the surface obtained from protein structures. CONCLUSION: This work presents a sequence-based method that takes into account surface information for predicting PPIs. The proposed procedure of surface identification improves the prediction performance with an F-measure of 5.1%. The extracted surfaces are also valuable in other biomedical applications that require similar information.
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spelling pubmed-30095012010-12-23 Predicting the protein-protein interactions using primary structures with predicted protein surface Chang, Darby Tien-Hao Syu, Yu-Tang Lin, Po-Chang BMC Bioinformatics Research BACKGROUND: Many biological functions involve various protein-protein interactions (PPIs). Elucidating such interactions is crucial for understanding general principles of cellular systems. Previous studies have shown the potential of predicting PPIs based on only sequence information. Compared to approaches that require other auxiliary information, these sequence-based approaches can be applied to a broader range of applications. RESULTS: This study presents a novel sequence-based method based on the assumption that protein-protein interactions are more related to amino acids at the surface than those at the core. The present method considers surface information and maintains the advantage of relying on only sequence data by including an accessible surface area (ASA) predictor recently proposed by the authors. This study also reports the experiments conducted to evaluate a) the performance of PPI prediction achieved by including the predicted surface and b) the quality of the predicted surface in comparison with the surface obtained from structures. The experimental results show that surface information helps to predict interacting protein pairs. Furthermore, the prediction performance achieved by using the surface estimated with the ASA predictor is close to that using the surface obtained from protein structures. CONCLUSION: This work presents a sequence-based method that takes into account surface information for predicting PPIs. The proposed procedure of surface identification improves the prediction performance with an F-measure of 5.1%. The extracted surfaces are also valuable in other biomedical applications that require similar information. BioMed Central 2010-01-18 /pmc/articles/PMC3009501/ /pubmed/20122202 http://dx.doi.org/10.1186/1471-2105-11-S1-S3 Text en Copyright ©2010 Chang et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Chang, Darby Tien-Hao
Syu, Yu-Tang
Lin, Po-Chang
Predicting the protein-protein interactions using primary structures with predicted protein surface
title Predicting the protein-protein interactions using primary structures with predicted protein surface
title_full Predicting the protein-protein interactions using primary structures with predicted protein surface
title_fullStr Predicting the protein-protein interactions using primary structures with predicted protein surface
title_full_unstemmed Predicting the protein-protein interactions using primary structures with predicted protein surface
title_short Predicting the protein-protein interactions using primary structures with predicted protein surface
title_sort predicting the protein-protein interactions using primary structures with predicted protein surface
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3009501/
https://www.ncbi.nlm.nih.gov/pubmed/20122202
http://dx.doi.org/10.1186/1471-2105-11-S1-S3
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