Asymmetry

Asymmetry analyzes amino acid substitution patterns in protein sequences to quantify directional substitutions between mesophilic and thermophilic organisms and reveal selection biases related to temperature adaptation.


Key Features:

  • AmbiguityRemover: Processes protein sequence alignments to eliminate ambiguously aligned sites and produce high-confidence alignment data.
  • AsymmetryCounter: Quantifies directional amino acid substitutions between pairs of protein sequences by identifying and counting non-symmetric amino acid replacements.
  • AsymmetryScaler: Aggregates and scales substitution counts from AsymmetryCounter to present substitutional asymmetry on a unified scale for comparative interpretation.

Scientific Applications:

  • Evolutionary and temperature-adaptation studies: Analyzes how amino acid substitution patterns differ between mesophiles and thermophiles to infer evolutionary pressures and selection biases.
  • Comparative genomics (Methanococcus vs Bacillus): Compares protein sequences from the archaeal genus Methanococcus and the bacterial genus Bacillus to detect dramatically asymmetrical substitution patterns between these genera.
  • Correlation with DNA G + C content: Investigates how differences in DNA G + C content may relate to observed asymmetrical amino acid substitution patterns.

Methodology:

Removes ambiguously aligned sites from protein sequence alignments; quantifies directional amino acid substitutions between sequence pairs by counting non-symmetric replacements; synthesizes substitution counts into a unified asymmetry scale.

Topics

Details

Tool Type:
desktop application
Operating Systems:
Windows, Mac
Added:
8/3/2017
Last Updated:
11/25/2024

Operations

Publications

McDonald JH, Grasso AM, Rejto LK. Patterns of temperature adaptation in proteins from Methanococcus and Bacillus. Molecular Biology and Evolution. 1999;16(12):1785-1790. doi:10.1093/oxfordjournals.molbev.a026090. PMID:10605119.

Documentation

Links