Predicting the disulfide bonding state of cysteines with combinations of kernel machines

  • Authors:
  • Alessio Ceroni;Paolo Frasconi;Andrea Passerini;Alessandro Vullo

  • Affiliations:
  • Dipartimento di Sistemi e Informatica, Università di Firenze, Italy;Department of Systems & Computer Science, University of Florence, Via di Santa Marta 3, I-50139 Firenze, Italy and Dipartimento di Sistemi e Informatica, Università di Firenze, Italy;Dipartimento di Sistemi e Informatica, Università di Firenze, Italy;Dipartimento di Sistemi e Informatica, Università di Firenze, Italy

  • Venue:
  • Journal of VLSI Signal Processing Systems - Special issue on signal processing and neural networks for bioinformatics
  • Year:
  • 2003

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Abstract

Cysteines may form covalent bonds, known as disulfide bridges, that have an important role in stabilizing the native conformation of proteins. Several methods have been proposed for predicting the bonding state of cysteines, either using local context or using global protein descriptors. In this paper we introduce an SVM based predictor that operates in two stages. The first stage is a multi-class classifier that operates at the protein level, using either standard Gaussian or spectrum kernels. The second stage is a binary classifier that refines the prediction by exploiting local context enriched with evolutionary information in the form of multiple alignment profiles. At both stages, we enriched profile encoding with information about cysteine conservation. The prediction accuracy of the system is 85% measured by 5-fold cross validation, on a set of 716 proteins from the September 2001 PDB Select dataset.