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Estimates the binding affinities between TPST-2 and various peptide substrates to differentiate sulfated and non-sulfated sequences that have been experimentally verified. Sulfation is an effective sulfation energy function based on physical interaction that combines both the energy cost for peptide local unfolding and the binding affinity. This method is also applicable to other posttranslational modification systems where the sequence or structural specificities are not well-defined.


Allows to identify tyrosine sulfation sites from primary protein sequences. PreSulSite adopts the secondary structure (SS), encoding based on group weight (EBGW), and autocorrelation functions (ACF) features to mine protein information. It can be useful in assisting the discovery of important protein modifications. The predictions are presented in a diagram that includes protein name, position of the site, flanking amino acids, and support vector machine (SVM) probability.