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Physicochemical Correlation between Amino Acid Sites in Short Sequences under Selective Pressure

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Bioinformatics Research and Applications (ISBRA 2008)

Part of the book series: Lecture Notes in Computer Science ((LNBI,volume 4983))

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Abstract

The activities and properties of proteins are the result of interactions among their constitutive amino acids. In the course of natural selection, substitutions which tend to destabilize a particular structure may be compensated by other substitutions which confer stability to that structure. Patterns of coordinated substitutions were studied in two sets of selected peptides. The first is a set of 181 amino acid sequences that were selected in vitro to bind a MHC class I molecule (Kb). The second is a set of 114 sequences of the Hypervariable Region 1 of Hepatitis C virus, which, originating from infected patients, result from natural selection in vivo. The patterns of coordinated substitutions in both datasets showed many significant structural and functional links between pairs of positions and conservation of specific selected physicochemical properties.

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Authors and Affiliations

  1. Molecular Epidemiology & Bioinformatics Laboratory, Division of Viral Hepatitis, Centers for Disease Control and Prevention, 1600 Clifton Rd, Atlanta, GA 30333

    David Campo, Zoya Dimitrova & Yuri Khudyakov

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  1. David Campo
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  2. Zoya Dimitrova
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  3. Yuri Khudyakov
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Ion Măndoiu Raj Sunderraman Alexander Zelikovsky

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Campo, D., Dimitrova, Z., Khudyakov, Y. (2008). Physicochemical Correlation between Amino Acid Sites in Short Sequences under Selective Pressure. In: Măndoiu, I., Sunderraman, R., Zelikovsky, A. (eds) Bioinformatics Research and Applications. ISBRA 2008. Lecture Notes in Computer Science(), vol 4983. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-79450-9_14

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  • DOI: https://doi.org/10.1007/978-3-540-79450-9_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-79449-3

  • Online ISBN: 978-3-540-79450-9

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