REPPER
REPPER: Fourier Transform and Self-Alignment Analysis of Protein Repeats
REPPER detects periodicities and internal repeats in protein sequences using Fourier Transform-based analysis and self-alignment strategies to identify short gapless repeats and repetitive structural motifs.
Key Features:
- FTwin (Fourier Transform-based Analysis): Applies Fourier Transform to protein sequences after assigning numerical values to amino acids based on physicochemical properties such as hydrophobicity, enabling detection of periodic patterns in the frequency domain.
- REPwin (Repeat-based Analysis): Performs self-alignments to identify and display significant internal similarities and repeat regions within protein sequences.
- Sliding Window Technique: Uses sliding window analysis in FTwin and REPwin to independently detect distinct periodic regions within the same protein sequence, improving sensitivity and specificity.
- Complementary Predictive Tools: Integrates secondary structure prediction (PSIPRED) and coiled coil prediction (COILS) to support structural interpretation of repetitive regions.
Scientific Applications:
- Protein Structure Analysis: Identifies short gapless repeats and periodicities to characterize structural organization and functional domains.
- Fibrous Protein Research: Analyzes repetitive motifs and coiled coil regions relevant to fibrous protein stability and architecture.
- Functional Annotation: Detects repeat regions associated with protein–protein interactions, aggregation properties, and domain architecture.
Methodology:
REPPER combines Fourier Transform-based frequency analysis of numerically encoded amino acid sequences with self-alignment-based repeat detection, applying a sliding window framework to resolve multiple periodic regions within individual proteins.
Topics
Details
- Tool Type:
- web application
- Added:
- 2/10/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Gruber M, Soding J, Lupas AN. REPPER--repeats and their periodicities in fibrous proteins. Nucleic Acids Research. 2005;33(Web Server):W239-W243. doi:10.1093/nar/gki405. PMID:15980460. PMCID:PMC1160166.