2D-MH

2D-MH generates two-dimensional graphical representations of protein sequences by mapping amino acid side-chain mass and hydrophobicity to analyze structural similarity and evolutionary relationships.


Key Features:

  • Two-Dimensional Sequence Representation: Constructs two-dimensional graphs of protein sequences using amino acid side-chain mass and hydrophobicity values.
  • Residue-Level Mapping: Maintains a one-to-one correspondence between each amino acid in the sequence and a point on the generated graphical curve.
  • Sequence Similarity Visualization: Enables visualization of structural similarities between protein sequences through comparison of two-dimensional curves.
  • Mutation Site Sensitivity: Detects sequence changes and mutation sites that may influence functional or drug-target regions.
  • Evolutionary Distance Measurement: Uses graphical sequence representations as a metric for estimating evolutionary distances between proteins from different species.

Scientific Applications:

  • Protein Sequence Analysis: Supports analysis of protein sequence characteristics using physicochemical property-based representations.
  • Comparative Protein Studies: Enables comparison of protein sequences to identify conserved regions and structural similarities.
  • Molecular Evolution Research: Facilitates estimation of evolutionary relationships between proteins across species.
  • Drug Target Investigation: Assists identification of mutation sites relevant to therapeutic targeting.

Methodology:

The tool encodes amino acid side-chain mass and hydrophobicity into two-dimensional coordinates to generate a continuous graphical curve representing the protein sequence with one-to-one correspondence between residues and plotted points.

Topics

Details

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

Operations

Publications

Wu Z, Xiao X, Chou K. 2D-MH: A web-server for generating graphic representation of protein sequences based on the physicochemical properties of their constituent amino acids. Journal of Theoretical Biology. 2010;267(1):29-34. doi:10.1016/j.jtbi.2010.08.007. PMID:20696175.

Documentation

Links