期刊
BIOINFORMATICS
卷 34, 期 5, 页码 875-877出版社
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/btx697
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资金
- Department of Science and Technology, Government of India [YSS/2014/000011]
We present a web-server for rapid prediction of changes in protein stabilities over a range of temperatures and experimental conditions upon single- or multiple-point substitutions of charged residues. Potential mutants are identified by a charge-shuffling procedure while the stability changes (i.e. an unfolding curve) are predicted employing an ensemble-based statistical-mechanical model. We expect this server to be a simple yet detailed tool for engineering stabilities, identifying electrostatically frustrated residues, generating local stability maps and in constructing fitness landscapes. The web-server is freely available at http://pbl.biotech.iitm.ac.in/pStab and supports recent versions of all major browsers.
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