iSulf-Cys

iSulf-Cys predicts cysteine S-sulfenylation sites in proteins to identify potential post-translational S-sulfenylation modifications involved in redox regulation.

Key Features:

• Physicochemical Properties Integration: Incorporates 14 distinct physicochemical properties of amino acids into its predictive model.
• Validation and Performance Metrics: Validated by 10-fold cross-validation over 20 iterations on the training dataset (AUC 0.7155 ± 0.0085; MCC 0.3122 ± 0.0144) and evaluated on independent testing (AUC 0.7343; MCC 0.3315).
• Feature Analysis: Constructs and analyzes features derived from both physicochemical properties and positional information within protein sequences.

Scientific Applications:

• Redox biology research: Identification of candidate S-sulfenylation sites to study redox-regulated protein functions.
• Protein chemistry and PTM mapping: Prediction of cysteine S-sulfenylation sites to aid characterization of post-translational modification landscapes.
• Disease mechanism investigation: Prioritization of sites for studies of pathologies linked to redox imbalance.
• Therapeutic research: Selection of modified cysteines for exploring targets and interventions involving specific protein modifications.

Methodology:

Features were constructed from 14 physicochemical properties and positional information, and model performance was assessed using 10-fold cross-validation over 20 iterations on the training dataset and independent testing.