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ProtDataTherm: A database for thermostability analysis and engineering of proteins
Protein thermostability engineering is a powerful tool to improve resistance of proteins against high temperatures and thereafter broaden their applications. For efficient protein thermostability engineering, different thermostability-classified data sources including sequences and 3D structures are...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5788348/ https://www.ncbi.nlm.nih.gov/pubmed/29377907 http://dx.doi.org/10.1371/journal.pone.0191222 |
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author | Pezeshgi Modarres, Hassan Mofrad, Mohammad R. Sanati-Nezhad, Amir |
author_facet | Pezeshgi Modarres, Hassan Mofrad, Mohammad R. Sanati-Nezhad, Amir |
author_sort | Pezeshgi Modarres, Hassan |
collection | PubMed |
description | Protein thermostability engineering is a powerful tool to improve resistance of proteins against high temperatures and thereafter broaden their applications. For efficient protein thermostability engineering, different thermostability-classified data sources including sequences and 3D structures are needed for different protein families. However, no data source is available providing such data easily. It is the first release of ProtDataTherm database for analysis and engineering of protein thermostability which contains more than 14 million protein sequences categorized based on their thermal stability and protein family. This database contains data needed for better understanding protein thermostability and stability engineering. Providing categorized protein sequences and structures as psychrophilic, mesophilic and thermophilic makes this database useful for the development of new tools in protein stability prediction. This database is available at http://profiles.bs.ipm.ir/softwares/protdatatherm. As a proof of concept, the thermostability that improves mutations were suggested for one sample protein belonging to one of protein families with more than 20 mesophilic and thermophilic sequences and with known experimentally measured ΔT of mutations available within ProTherm database. |
format | Online Article Text |
id | pubmed-5788348 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57883482018-02-09 ProtDataTherm: A database for thermostability analysis and engineering of proteins Pezeshgi Modarres, Hassan Mofrad, Mohammad R. Sanati-Nezhad, Amir PLoS One Research Article Protein thermostability engineering is a powerful tool to improve resistance of proteins against high temperatures and thereafter broaden their applications. For efficient protein thermostability engineering, different thermostability-classified data sources including sequences and 3D structures are needed for different protein families. However, no data source is available providing such data easily. It is the first release of ProtDataTherm database for analysis and engineering of protein thermostability which contains more than 14 million protein sequences categorized based on their thermal stability and protein family. This database contains data needed for better understanding protein thermostability and stability engineering. Providing categorized protein sequences and structures as psychrophilic, mesophilic and thermophilic makes this database useful for the development of new tools in protein stability prediction. This database is available at http://profiles.bs.ipm.ir/softwares/protdatatherm. As a proof of concept, the thermostability that improves mutations were suggested for one sample protein belonging to one of protein families with more than 20 mesophilic and thermophilic sequences and with known experimentally measured ΔT of mutations available within ProTherm database. Public Library of Science 2018-01-29 /pmc/articles/PMC5788348/ /pubmed/29377907 http://dx.doi.org/10.1371/journal.pone.0191222 Text en © 2018 Pezeshgi Modarres et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Pezeshgi Modarres, Hassan Mofrad, Mohammad R. Sanati-Nezhad, Amir ProtDataTherm: A database for thermostability analysis and engineering of proteins |
title | ProtDataTherm: A database for thermostability analysis and engineering of proteins |
title_full | ProtDataTherm: A database for thermostability analysis and engineering of proteins |
title_fullStr | ProtDataTherm: A database for thermostability analysis and engineering of proteins |
title_full_unstemmed | ProtDataTherm: A database for thermostability analysis and engineering of proteins |
title_short | ProtDataTherm: A database for thermostability analysis and engineering of proteins |
title_sort | protdatatherm: a database for thermostability analysis and engineering of proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5788348/ https://www.ncbi.nlm.nih.gov/pubmed/29377907 http://dx.doi.org/10.1371/journal.pone.0191222 |
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