Protein data condensation for effective quaternary structure classification

  • Authors:
  • Fabrizio Angiulli;Valeria Fionda;Simona E. Rombo

  • Affiliations:
  • DEIS, Università della Calabria, Rende, CS, Italy;Dept. of Mathematics, Rende, CS, Italy;DEIS, Università della Calabria, Rende, CS, Italy

  • Venue:
  • IDEAL'07 Proceedings of the 8th international conference on Intelligent data engineering and automated learning
  • Year:
  • 2007

Quantified Score

Hi-index 0.00

Visualization

Abstract

Many proteins are composed of two or more subunits, each associated with different polypeptide chains. The number and the arrangement of subunits forming a protein are referred to as quaternary structure. The quaternary structure of a protein is important, since it characterizes the biological function of the protein when it is involved in specific biological processes. Unfortunately, quaternary structures are not trivially deducible from protein amino acid sequences. In this work, we propose a protein quaternary structure classification method exploiting the functional domain composition of proteins. It is based on a nearest neighbor condensation technique in order to reduce both the portion of dataset to be stored and the number of comparisons to carry out. Our approach seems to be promising, in that it guarantees an high classification accuracy, even though it does not require the entire dataset to be analyzed. Indeed, experimental evaluations show that the method here proposed selects a small dataset portion for the classification (of the order of the 6.43%) and that it is very accurate (97.74%).