SCooP is a fast and accurate method for predicting the Gibbs-Helmholtz equation associated to the folding transition of a target protein of known (or modeled) structure. In addition, SCooP yields an estimation of the thermodynamic quantities that characterize the folding process, in particular the change in enthalpy and in heat capacity upon folding, the melting temperature and the folding free energy at room temperature.

The input information required by SCooP is the protein structure that is uploaded either manually or from the Protein Data Bank. Using standard knowledge-based statistical potential as well as recently introduced temperature-dependent potentials, SCooP outputs the full temperature-dependence of the folding free energy.

The core of the webserver consists of a Query page where the user submits the necessary information about the target protein and a Curve page in which the values of the thermodynamic quantities and the graphical illustration of the Gibbs-Helmholtz equation are shown. There is moreover a Help page in which information about the queries, computation, results and perspectives is given.

News (06-20): After a major webserver issue that has been now completely solved, SCooP has been upgraded by adding the environmental temperatures of about 14000 new host organisms.

1) F. Pucci, M. Rooman (2014), Stability Curve Prediction for homologous proteins using temperature-dependent statistical potentials, PLoS Computational Biology 10, e1003689.

2) F. Pucci, M. Rooman (2016), Towards an accurate prediction of the thermal stability of homologous proteins, Journal of Biomolecular Structure and Dynamics 34, 1132-42.

3) F. Pucci, J.M. Kwasigroch, M. Rooman (2017), SCooP : an accurate and fast predictor of protein stability curves as a function of the temperature, Bioinformatics 33, 3415-3422.