DispHScan

DispHScan predicts pH-dependent protein disorder to identify pH-induced disorder–order transitions across multiple sequences for studies of intrinsically disordered proteins (IDPs) and proteome-scale analyses.

Key Features:

• pH-Dependent Disorder Prediction: Uses a charge-hydrophobicity diagram to model the influence of solution pH on protein conformational states and predict disorder–order transitions.
• Multi-Sequence Analysis: Analyzes multiple sequences simultaneously to enable proteome-wide studies and screening of mutant collections.
• Spot Folding Transition Identification: Detects local pH-driven spot folding transitions across large datasets.

Scientific Applications:

• Physiological and Pathological Studies: Investigates the role of pH-modulated conditional disorder in cellular and disease contexts.
• IDP Conformational Analysis: Assesses solvent-dependent conformational switches of intrinsically disordered proteins that affect their activity.
• Proteome-Scale Screening: Identifies pH-sensitive regions in proteome-wide datasets and collections of mutants, including relevance to biotechnological production processes.

Methodology:

Computational modeling integrates a charge–hydrophobicity diagram with solution pH variations to predict disorder–order transitions.