DispHred

DispHred predicts pH-dependent order–disorder transitions in intrinsically disordered proteins (IDPs) by evaluating the charge–hydropathy relationship as a function of pH.


Key Features:

  • Charge–Hydropathy (C-H) analysis: Evaluates sequence disorder using the charge–hydropathy relationship to distinguish ordered versus disordered states as a function of pH.
  • pH-dependent net charge and hydrophobicity: Computes protein net charge and hydrophobicity values that vary with solution pH.
  • Sliding-window calculation: Applies a sliding window along the sequence to obtain local charge and hydrophobicity estimates for region-specific predictions.
  • Order–disorder transition prediction: Predicts transitions between ordered and disordered states across different pH conditions.
  • Conditional disorder detection: Identifies conditionally disordered segments that change structural state in response to pH.
  • Design support for disorder tags: Assesses pH-dependent disorder properties to inform synthetic design of disorder tags for biotechnological applications.
  • Integration with hydrophobicity-based algorithms: Provides pH-adjusted hydrophobicity inputs compatible with other algorithms that use hydrophobicity as a parameter.

Scientific Applications:

  • Characterization of IDP behavior: Investigates how pH modulates net charge, hydrophobicity, and resulting order–disorder behavior in intrinsically disordered proteins.
  • Analysis of conditionally disordered segments: Maps sequence regions that undergo pH-induced structural transitions for functional or regulatory studies.
  • Design of disorder tags: Guides the synthetic design of pH-responsive disorder tags for biotechnology.
  • Enhanced bioinformatics pipelines: Supplies pH-dependent hydrophobicity information for incorporation into hydrophobicity-based computational workflows.

Methodology:

Performs a charge–hydropathy (C-H) analysis by computing net charge and hydrophobicity as functions of pH and applying a sliding-window calculation along the sequence to predict pH-dependent order–disorder transitions.

Topics

Details

Tool Type:
web application
Added:
1/18/2021
Last Updated:
3/1/2021

Operations

Publications

Santos J, Iglesias V, Pintado C, Santos-Suárez J, Ventura S. DispHred: A Server to Predict pH-Dependent Order–Disorder Transitions in Intrinsically Disordered Proteins. International Journal of Molecular Sciences. 2020;21(16):5814. doi:10.3390/ijms21165814. PMID:32823616. PMCID:PMC7461198.

PMID: 32823616
PMCID: PMC7461198
Funding: - Ministerio de Ciencia y Tecnología: BIO2016-78310-R - Institució Catalana de Recerca i Estudis Avançats: ICREA-Academia 2015 - Ministerio de Ciencia e Innovación: FPU17/01157