Transmembrane helix prediction in proteins using hydrophobicity properties and higher-order statistics

Ilias K. Kitsas, Leontios J. Hadjileontiadis, Stavros M. Panas

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Prediction of the transmembrane (TM) helices is important in the study of membrane proteins. A novel method to predict the location and length of both single and multiple TM helices in human proteins is presented. The proposed method is based on a combination of hydrophobicity and higher-order statistics, resulting in a TM prediction tool, namely K4 HTM. A training dataset of 117 human single TM proteins and two test-datasets containing 499 and 484 human single and multiple TM proteins, respectively, were drawn from the SWISS-PROT public database and used for the optimisation and evaluation of K4 HTM. Validation results showed that K4 HTM correctly predicts the entire topology for 99.68% and 93.08% of the sequences in the single and multiple test-datasets, respectively. These results compare favourably with existing methods, such as SPLIT4, TMHMM2, WAVETM and SOSUI, constituting an alternative approach to the TM helix prediction problem.

Original languageBritish English
Pages (from-to)867-880
Number of pages14
JournalComputers in Biology and Medicine
Volume38
Issue number8
DOIs
StatePublished - Aug 2008

Keywords

  • Hydrophobicity
  • Kurtosis
  • Membrane protein
  • Prediction
  • Transmembrane helix

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