ProtDataTherm: A database for thermostability analysis and engineering of proteins

Journal Article · 29 January 2018 · PLoS ONE

DOI: https://doi.org/10.1371/journal.pone.0191222 · OSTI ID:1627852

Pezeshgi Modarres, Hassan ^[1]; Mofrad, Mohammad R. ^[2]; Sanati-Nezhad, Amir  ^[3]

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1. Univ. of Calgary, AB (Canada). Dept. of Mechanical and Manufacturing Engineering. BioMEMS and Bioinspired Microfluidic Lab.; Univ. of California, Berkeley, CA (United States). Depts. of Bioengineering and Mechanical Engineering. Molecular Cell Biomechanics Lab.; Inst. for Research in Fundamental Sciences (IPM), Tehran (Iran). School of Biological Sciences
2. Univ. of California, Berkeley, CA (United States). Depts. of Bioengineering and Mechanical Engineering. Molecular Cell Biomechanics Lab.; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Physical Biosciences Division
3. Univ. of Calgary, AB (Canada). Dept. of Mechanical and Manufacturing Engineering. BioMEMS and Bioinspired Microfluidic Lab.; Univ. of Calgary, AB (Canada). Center for BioEngineering Research and Education

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.

• Research Organization: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
• Sponsoring Organization: USDOE Office of Science (SC)
• Grant/Contract Number: AC02-05CH11231
• OSTI ID: 1627852
• Journal Information: PLoS ONE, Vol. 13, Issue 1; ISSN 1932-6203
• Publisher: Public Library of ScienceCopyright Statement
• Country of Publication: United States
• Language: English