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NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically disordered regions. These segments are involved in binding to partner molecules...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society of Japan
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692026/ https://www.ncbi.nlm.nih.gov/pubmed/33304713 http://dx.doi.org/10.2142/biophysico.BSJ-2020026 |
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author | Anbo, Hiroto Amagai, Hiroki Fukuchi, Satoshi |
author_facet | Anbo, Hiroto Amagai, Hiroki Fukuchi, Satoshi |
author_sort | Anbo, Hiroto |
collection | PubMed |
description | Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically disordered regions. These segments are involved in binding to partner molecules, such as protein and DNA, and play important roles in signaling pathways and/or transcriptional regulation. Although there are databases that gather information on such disordered binding regions, data remain limited. Therefore, it is desirable to develop programs to predict the disordered binding regions without using data for the binding regions. We developed a program, NeProc, to predict the disordered binding regions, which can be regarded as intrinsically disordered regions with a structural propensity. We only used data for the structural domains and intrinsically disordered regions to detect such regions. NeProc accepts a query amino acid sequence converted into a position specific score matrix, and uses two neural networks that employ different window sizes, a neural network of short windows, and a neural network of long windows. The performance of NeProc was comparable to that of existing programs of the disordered binding region prediction. This result presents the possibility to overcome the shortage of the disordered binding region data in the development of the prediction programs for these binding regions. NeProc is available at http://flab.neproc.org/neproc/index.html |
format | Online Article Text |
id | pubmed-7692026 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Biophysical Society of Japan |
record_format | MEDLINE/PubMed |
spelling | pubmed-76920262020-12-09 NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences Anbo, Hiroto Amagai, Hiroki Fukuchi, Satoshi Biophys Physicobiol Database and Computer Program Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically disordered regions. These segments are involved in binding to partner molecules, such as protein and DNA, and play important roles in signaling pathways and/or transcriptional regulation. Although there are databases that gather information on such disordered binding regions, data remain limited. Therefore, it is desirable to develop programs to predict the disordered binding regions without using data for the binding regions. We developed a program, NeProc, to predict the disordered binding regions, which can be regarded as intrinsically disordered regions with a structural propensity. We only used data for the structural domains and intrinsically disordered regions to detect such regions. NeProc accepts a query amino acid sequence converted into a position specific score matrix, and uses two neural networks that employ different window sizes, a neural network of short windows, and a neural network of long windows. The performance of NeProc was comparable to that of existing programs of the disordered binding region prediction. This result presents the possibility to overcome the shortage of the disordered binding region data in the development of the prediction programs for these binding regions. NeProc is available at http://flab.neproc.org/neproc/index.html The Biophysical Society of Japan 2020-11-03 /pmc/articles/PMC7692026/ /pubmed/33304713 http://dx.doi.org/10.2142/biophysico.BSJ-2020026 Text en 2020 THE BIOPHYSICAL SOCIETY OF JAPAN https://creativecommons.org/licenses/by-nc-sa/4.0/This article is licensed under the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. To view a copy of this license, visit
https://creativecommons.org/licenses/by-nc-sa/4.0/. |
spellingShingle | Database and Computer Program Anbo, Hiroto Amagai, Hiroki Fukuchi, Satoshi NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
title | NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
title_full | NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
title_fullStr | NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
title_full_unstemmed | NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
title_short | NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
title_sort | neproc predicts binding segments in intrinsically disordered regions without learning binding region sequences |
topic | Database and Computer Program |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692026/ https://www.ncbi.nlm.nih.gov/pubmed/33304713 http://dx.doi.org/10.2142/biophysico.BSJ-2020026 |
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