Exploring protein's optimal HP configurations by self-organizing mapping

J Bioinform Comput Biol. 2005 Apr;3(2):385-400. doi: 10.1142/s0219720005001107.

Abstract

Self-organizing map (SOM) has been used in protein folding prediction when the HP model is employed. The existing work uses a square-like shape lattice with l = m x n points to represent the optimal compact structure of a sequence of l amino acids. In this paper, a general l'-size sequence of amino acids is self-organized in a two dimensional lattice with l (> l') points. The obtained minimum configuration then has a flexible shape, in contrast to the compact structure limited in the lattice. To fulfil this extension, a new self-organizing map (SOM) technique is proposed to deal with the difficulty of the unsymmetric input and output spaces. New competition rules in the training phase are introduced and a local search method is applied to overcome the multi-mapping phenomena. Several HP benchmark examples with up to 36 amino acids are tested to verify the effectiveness of the proposed approach in this paper.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms*
  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Artificial Intelligence*
  • Computer Simulation
  • Hydrophobic and Hydrophilic Interactions
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Proteins / analysis
  • Proteins / chemistry*
  • Proteins / classification
  • Sequence Analysis, Protein / methods*
  • Static Electricity
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Proteins