pStab: prediction of stable mutants, unfolding curves, stability maps and protein electrostatic frustration

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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.

Availability and implementation

The web-server is freely available at and supports recent versions of all major browsers.


Supplementary information

Supplementary data are available at Bioinformatics online.

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