PREDICTION OF CHIMERIC PROTEIN FOLD

Ruben Acuna*, Zoe Lacroix, Fayez Hadji, Jacques Chomilier, Nikolaos Papandreou

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract / Description of output

We propose two computational methods for predicting if a protein produced by fusion of genes will conserve the structures of the fused proteins. We use two complementary paths for prediction. The former is a simulation from the sequence while the latter exploits its expected structure. Early stages of protein folding are simulated from their amino acid sequence by capturing the most interacting residues (MIR). Individual domain structures (or models) are superposed onto the predicted complex structure (or model). When no structure exists, a model is calculated using a set of ab initio and fold recognition tools. These results are used to predict the validity of the chimeric protein. We test the two methods against a dataset of 10 proteins.

Original languageEnglish
Title of host publicationBIOINFORMATICS: PROCEEDINGS OF THE INTERNATIONAL CONFERENCE ON BIOINFORMATICS MODELS, METHODS AND ALGORITHMS
EditorsC Correia, A Fred, H Gamboa, J Schier
PublisherSCITEPRESS
Pages234-239
Number of pages6
DOIs
Publication statusPublished - 2012
EventInternational Conference on Bioinformatics Models, Methods and Algorithms (BIOINFORMATICS) - Algarve, Portugal
Duration: 1 Feb 20124 Feb 2012

Conference

ConferenceInternational Conference on Bioinformatics Models, Methods and Algorithms (BIOINFORMATICS)
Country/TerritoryPortugal
Period1/02/124/02/12

Keywords / Materials (for Non-textual outputs)

  • Chimeric Proteins
  • Folding
  • Prediction
  • Simulation
  • Fusion Proteins
  • MIR

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