assp

assp assesses residue-by-residue accuracy of consensus secondary structure predictions derived from multiple protein sequence alignments to evaluate agreement between predicted and actual structures within homologous protein families.


Key Features:

  • Accuracy Estimation: Estimates the range of expected residue-by-residue accuracies for secondary structure predictions derived from multiple protein sequence alignments.
  • Analysis of Structural Families: Leverages analysis of known protein structural families to determine achievable prediction accuracies across homologous proteins.
  • Consensus Prediction Evaluation: Provides expected agreement levels between consensus secondary structure predictions and individual protein members within an alignment.
  • Domain-specific Validation: Applied to specific protein domains such as annexins, SH2 domains, and SH3 domains to validate predicted accuracy ranges against empirical structures.

Scientific Applications:

  • Structural Biology: Enables evaluation of secondary structure prediction reliability to inform protein folding and structure–function studies.
  • Protein Engineering: Informs how sequence modifications may affect secondary structure by estimating prediction accuracy and variability.
  • Comparative Genomics: Supports comparison of protein secondary structure predictions across species and within homologous families.

Methodology:

Analyzes multiple protein sequence alignments and known protein structural families, using empirical data from known protein structures to determine expected ranges of secondary structure prediction accuracy.

Topics

Details

Tool Type:
command-line tool
Operating Systems:
Linux
Added:
8/3/2017
Last Updated:
11/25/2024

Operations

Data Inputs & Outputs

Protein sequence analysis

Inputs

    Outputs

    Other operations do not define inputs or outputs.

    Publications

    Russell RB, Barton GJ. The Limits of Protein Secondary Structure Prediction Accuracy from Multiple Sequence Alignment. Journal of Molecular Biology. 1993;234(4):951-957. doi:10.1006/jmbi.1993.1649. PMID:8263941.

    Documentation

    Links