HELIQUEST
HELIQUEST analyzes alpha-helices in protein sequences and structures by calculating their physicochemical properties and amino acid composition to identify and screen helix-like segments in protein databases.
Key Features:
- Physicochemical property calculation: Computes physicochemical properties of alpha-helices and reports amino acid composition.
- Helix identification: Screens protein databases to identify segments that exhibit similar helix features.
- Manual mutation: Supports manual mutation of helix sequences for targeted sequence changes.
- Automatic mutation: Performs automatic mutations using a genetic algorithm approach.
- Sequence optimization: Iteratively optimizes sequences to design helix analogues based on predefined criteria.
Scientific Applications:
- Structural biology: Supports analysis of alpha-helix contributions to protein structure and structure–function relationships.
- Protein engineering: Enables design and optimization of helical sequences for protein engineering applications.
- Computational chemistry: Assists computational studies of peptide and protein helices.
- Comparative analysis and functional prediction: Facilitates comparative screening of helix-like segments across databases to aid functional predictions.
- Rational design: Aids rational design of proteins with tailored properties for industrial, medical, or academic purposes.
Methodology:
Calculates physicochemical properties and amino acid composition of helices, screens protein databases for similar helix segments, and performs manual or genetic-algorithm-based automatic mutations with iterative sequence optimization using predefined criteria.
Topics
Details
- Tool Type:
- web application
- Operating Systems:
- Linux, Windows, Mac
- Added:
- 4/21/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Gautier R, Douguet D, Antonny B, Drin G. HELIQUEST: a web server to screen sequences with specific α-helical properties. Bioinformatics. 2008;24(18):2101-2102. doi:10.1093/bioinformatics/btn392. PMID:18662927.
PMID: 18662927