Literature DB >> 17688314

A hidden Markov model for predicting protein interfaces.

Cao Nguyen1, Katheleen J Gardiner, Krzysztof J Cios.   

Abstract

Protein-protein interactions play a defining role in protein function. Identifying the sites of interaction in a protein is a critical problem for understanding its functional mechanisms, as well as for drug design. To predict sites within a protein chain that participate in protein complexes, we have developed a novel method based on the Hidden Markov Model, which combines several biological characteristics of the sequences neighboring a target residue: structural information, accessible surface area, and transition probability among amino acids. We have evaluated the method using 5-fold cross-validation on 139 unique proteins and demonstrated precision of 66% and recall of 61% in identifying interfaces. These results are better than those achieved by other methods used for identification of interfaces.

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Year:  2007        PMID: 17688314     DOI: 10.1142/s0219720007002722

Source DB:  PubMed          Journal:  J Bioinform Comput Biol        ISSN: 0219-7200            Impact factor:   1.122


  2 in total

1.  Efficient algorithms for training the parameters of hidden Markov models using stochastic expectation maximization (EM) training and Viterbi training.

Authors:  Tin Y Lam; Irmtraud M Meyer
Journal:  Algorithms Mol Biol       Date:  2010-12-09       Impact factor: 1.405

2.  HMMCONVERTER 1.0: a toolbox for hidden Markov models.

Authors:  Tin Yin Lam; Irmtraud M Meyer
Journal:  Nucleic Acids Res       Date:  2009-11       Impact factor: 16.971

  2 in total

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