PeSA
PeSA analyzes peptide arrays, permutation arrays, and One-Probe Arrays with Labeled peptides (OPALs) to generate motifs and position-specific scoring matrices (PSSMs) for peptide specificity studies, supporting interpretation of protein-protein interactions, enzyme-substrate specificity, and epigenetic modification sites.
Key Features:
- Motif generation (PSSMs): Generates position-specific scoring matrices that represent candidate interaction motifs from peptide data.
- Array type support: Processes data from peptide arrays, permutation arrays, and One-Probe Arrays with Labeled peptides (OPALs).
- Frequency-based model: Identifies residue patterns by analyzing residue occurrence across a provided list of peptides using frequency criteria.
- Weight-based model: Constructs motifs from quantified matrices by assigning positional weights to residues.
- Threshold-based filtering: Populates lists of peptides that match predefined thresholds derived from quantified matrices.
Scientific Applications:
- Protein-protein interaction analysis: Identifies candidate interaction motifs relevant to PPIs from peptide array experiments.
- Enzyme-substrate specificity: Characterizes positional residue preferences that inform enzyme substrate recognition and specificity.
- Epigenetic modification site analysis: Aids detection of motifs associated with epigenetic modification sites.
- Peptide specificity studies: Supports discovery of candidate motifs and specificity determinants from peptide array datasets.
Methodology:
Generates PSSMs; applies a frequency-based model that analyzes residue occurrence across peptide lists; applies a weight-based model that uses quantified matrices to compute positional weights; and performs threshold-based filtering to select peptides meeting predefined criteria.
Topics
Details
- License:
- GPL-3.0
- Programming Languages:
- C#
- Added:
- 11/14/2019
- Last Updated:
- 1/9/2021
Operations
Publications
Topcu E, Biggar KK. PeSA: A Software Tool for Peptide Specificity Analysis. Unknown Journal. 2019. doi:10.1101/760140.