OsFP: A web server for predicting the oligomeric states of fluorescent proteins

© 2016 The Author(s). Background: Currently, monomeric fluorescent proteins (FP) are ideal markers for protein tagging. The prediction of oligomeric states is helpful for enhancing live biomedical imaging. Computational prediction of FP oligomeric states can accelerate the effort of protein engineer...

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Main Authors: Saw Simeon, Watshara Shoombuatong, Nuttapat Anuwongcharoen, Likit Preeyanon, Virapong Prachayasittikul, Jarl E.S. Wikberg, Chanin Nantasenamat
Other Authors: Mahidol University
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Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/43417
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spelling th-mahidol.434172019-03-14T15:04:29Z OsFP: A web server for predicting the oligomeric states of fluorescent proteins Saw Simeon Watshara Shoombuatong Nuttapat Anuwongcharoen Likit Preeyanon Virapong Prachayasittikul Jarl E.S. Wikberg Chanin Nantasenamat Mahidol University Uppsala Universitet Chemistry Computer Science © 2016 The Author(s). Background: Currently, monomeric fluorescent proteins (FP) are ideal markers for protein tagging. The prediction of oligomeric states is helpful for enhancing live biomedical imaging. Computational prediction of FP oligomeric states can accelerate the effort of protein engineering efforts of creating monomeric FPs. To the best of our knowledge, this study represents the first computational model for predicting and analyzing FP oligomerization directly from the amino acid sequence. Results: After data curation, an exhaustive data set consisting of 397 non-redundant FP oligomeric states was compiled from the literature. Results from benchmarking of the protein descriptors revealed that the model built with amino acid composition descriptors was the top performing model with accuracy, sensitivity and specificity in excess of 80% and MCC greater than 0.6 for all three data subsets (e.g. training, tenfold cross-validation and external sets). The model provided insights on the important residues governing the oligomerization of FP. To maximize the benefit of the generated predictive model, it was implemented as a web server under the R programming environment. Conclusion: osFP affords a user-friendly interface that can be used to predict the oligomeric state of FP using the protein sequence. The advantage of osFP is that it is platform-independent meaning that it can be accessed via a web browser on any operating system and device. osFP is freely accessible at http://codes.bio/osfp/ while the source code and data set is provided on GitHub at https://github.com/chaninn/osFP/. Graphical Abstract. 2018-12-11T02:31:42Z 2019-03-14T08:04:29Z 2018-12-11T02:31:42Z 2019-03-14T08:04:29Z 2016-12-20 Article Journal of Cheminformatics. Vol.8, No.1 (2016) 10.1186/s13321-016-0185-8 17582946 2-s2.0-85006380259 https://repository.li.mahidol.ac.th/handle/123456789/43417 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85006380259&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Chemistry
Computer Science
spellingShingle Chemistry
Computer Science
Saw Simeon
Watshara Shoombuatong
Nuttapat Anuwongcharoen
Likit Preeyanon
Virapong Prachayasittikul
Jarl E.S. Wikberg
Chanin Nantasenamat
OsFP: A web server for predicting the oligomeric states of fluorescent proteins
description © 2016 The Author(s). Background: Currently, monomeric fluorescent proteins (FP) are ideal markers for protein tagging. The prediction of oligomeric states is helpful for enhancing live biomedical imaging. Computational prediction of FP oligomeric states can accelerate the effort of protein engineering efforts of creating monomeric FPs. To the best of our knowledge, this study represents the first computational model for predicting and analyzing FP oligomerization directly from the amino acid sequence. Results: After data curation, an exhaustive data set consisting of 397 non-redundant FP oligomeric states was compiled from the literature. Results from benchmarking of the protein descriptors revealed that the model built with amino acid composition descriptors was the top performing model with accuracy, sensitivity and specificity in excess of 80% and MCC greater than 0.6 for all three data subsets (e.g. training, tenfold cross-validation and external sets). The model provided insights on the important residues governing the oligomerization of FP. To maximize the benefit of the generated predictive model, it was implemented as a web server under the R programming environment. Conclusion: osFP affords a user-friendly interface that can be used to predict the oligomeric state of FP using the protein sequence. The advantage of osFP is that it is platform-independent meaning that it can be accessed via a web browser on any operating system and device. osFP is freely accessible at http://codes.bio/osfp/ while the source code and data set is provided on GitHub at https://github.com/chaninn/osFP/. Graphical Abstract.
author2 Mahidol University
author_facet Mahidol University
Saw Simeon
Watshara Shoombuatong
Nuttapat Anuwongcharoen
Likit Preeyanon
Virapong Prachayasittikul
Jarl E.S. Wikberg
Chanin Nantasenamat
format Article
author Saw Simeon
Watshara Shoombuatong
Nuttapat Anuwongcharoen
Likit Preeyanon
Virapong Prachayasittikul
Jarl E.S. Wikberg
Chanin Nantasenamat
author_sort Saw Simeon
title OsFP: A web server for predicting the oligomeric states of fluorescent proteins
title_short OsFP: A web server for predicting the oligomeric states of fluorescent proteins
title_full OsFP: A web server for predicting the oligomeric states of fluorescent proteins
title_fullStr OsFP: A web server for predicting the oligomeric states of fluorescent proteins
title_full_unstemmed OsFP: A web server for predicting the oligomeric states of fluorescent proteins
title_sort osfp: a web server for predicting the oligomeric states of fluorescent proteins
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/43417
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