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Markov analysis of alpha-helical, beta-sheet and random coil regions of proteins

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Lettere al Nuovo Cimento (1971-1985)

Summary

The rules up to now used to predict the spatial configuration of proteins from their primary structure are mostly based on the recurrence analysis of some doublets, triplets and so on of contiguous amino acids, but they do not take into account the correlation characteristics of the whole amino acid sequence.

We have carried out a statistical analysis of amino acid sequences for the alphahelical, beta-sheet and random coil regions of about twenty proteins with known secondary structure by considering correlation effects.

Our results demonstrate that these sequences are at least a second-order Markov chain,i.e. they appear as if they were generated by a source that remembers at least the two aminoacids before the one being generated and that these two previous symbols influence the present choice.

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Authors and Affiliations

  1. Istituto di Fisica Sperimentale, Mostra d’Oltre Mare, Pad. 20, Napoli

    M. Macchiato

  2. Istituto di Genetica e Biofisica, Via Marconi 10, Napoli

    A. Tramontano

Authors
  1. M. Macchiato
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  2. A. Tramontano
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Macchiato, M., Tramontano, A. Markov analysis of alpha-helical, beta-sheet and random coil regions of proteins. Lett. Nuovo Cimento 37, 89–94 (1983). https://doi.org/10.1007/BF02747254

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  • DOI: https://doi.org/10.1007/BF02747254

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