CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins

© 2017 Reny Pratiwi et al. Antifreeze protein (AFP) is an ice-binding protein that protects organisms from freezing in extremely cold environments. AFPs are found across a diverse range of species and, therefore, significantly differ in their structures. As there are no consensus sequences available...

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Main Authors: Reny Pratiwi, Aijaz Ahmad Malik, Nalini Schaduangrat, Virapong Prachayasittikul, Jarl E.S. Wikberg, Chanin Nantasenamat, Watshara Shoombuatong
Other Authors: Mahidol University
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Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/42276
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spelling th-mahidol.422762019-03-14T15:03:19Z CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins Reny Pratiwi Aijaz Ahmad Malik Nalini Schaduangrat Virapong Prachayasittikul Jarl E.S. Wikberg Chanin Nantasenamat Watshara Shoombuatong Mahidol University Setia Budi University Uppsala Biomedicinska Centrum Chemistry © 2017 Reny Pratiwi et al. Antifreeze protein (AFP) is an ice-binding protein that protects organisms from freezing in extremely cold environments. AFPs are found across a diverse range of species and, therefore, significantly differ in their structures. As there are no consensus sequences available for determining the ice-binding domain of AFPs, thus the prediction and characterization of AFPs from their sequence is a challenging task. This study addresses this issue by predicting AFPs directly from sequence on a large set of 478 AFPs and 9,139 non-AFPs using machine learning (e.g., random forest) as a function of interpretable features (e.g., amino acid composition, dipeptide composition, and physicochemical properties). Furthermore, AFPs were characterized using propensity scores and important physicochemical properties via statistical and principal component analysis. The predictive model afforded high performance with an accuracy of 88.28% and results revealed that AFPs are likely to be composed of hydrophobic amino acids as well as amino acids with hydroxyl and sulfhydryl side chains. The predictive model is provided as a free publicly available web server called CryoProtect for classifying query protein sequence as being either AFP or non-AFP. The data set and source code are for reproducing the results which are provided on GitHub. 2018-12-21T07:15:40Z 2019-03-14T08:03:19Z 2018-12-21T07:15:40Z 2019-03-14T08:03:19Z 2017-01-01 Article Journal of Chemistry. Vol.2017, (2017) 10.1155/2017/9861752 20909071 20909063 2-s2.0-85013322071 https://repository.li.mahidol.ac.th/handle/123456789/42276 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85013322071&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
spellingShingle Chemistry
Reny Pratiwi
Aijaz Ahmad Malik
Nalini Schaduangrat
Virapong Prachayasittikul
Jarl E.S. Wikberg
Chanin Nantasenamat
Watshara Shoombuatong
CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins
description © 2017 Reny Pratiwi et al. Antifreeze protein (AFP) is an ice-binding protein that protects organisms from freezing in extremely cold environments. AFPs are found across a diverse range of species and, therefore, significantly differ in their structures. As there are no consensus sequences available for determining the ice-binding domain of AFPs, thus the prediction and characterization of AFPs from their sequence is a challenging task. This study addresses this issue by predicting AFPs directly from sequence on a large set of 478 AFPs and 9,139 non-AFPs using machine learning (e.g., random forest) as a function of interpretable features (e.g., amino acid composition, dipeptide composition, and physicochemical properties). Furthermore, AFPs were characterized using propensity scores and important physicochemical properties via statistical and principal component analysis. The predictive model afforded high performance with an accuracy of 88.28% and results revealed that AFPs are likely to be composed of hydrophobic amino acids as well as amino acids with hydroxyl and sulfhydryl side chains. The predictive model is provided as a free publicly available web server called CryoProtect for classifying query protein sequence as being either AFP or non-AFP. The data set and source code are for reproducing the results which are provided on GitHub.
author2 Mahidol University
author_facet Mahidol University
Reny Pratiwi
Aijaz Ahmad Malik
Nalini Schaduangrat
Virapong Prachayasittikul
Jarl E.S. Wikberg
Chanin Nantasenamat
Watshara Shoombuatong
format Article
author Reny Pratiwi
Aijaz Ahmad Malik
Nalini Schaduangrat
Virapong Prachayasittikul
Jarl E.S. Wikberg
Chanin Nantasenamat
Watshara Shoombuatong
author_sort Reny Pratiwi
title CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins
title_short CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins
title_full CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins
title_fullStr CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins
title_full_unstemmed CryoProtect: A Web Server for Classifying Antifreeze Proteins from Nonantifreeze Proteins
title_sort cryoprotect: a web server for classifying antifreeze proteins from nonantifreeze proteins
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/42276
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