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Singular hydrophobicity patterns and net charge: a mesoscopic principle for protein aggregation/folding

Author

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  • Zbilut, Joseph P.
  • Mitchell, Julie C.
  • Giuliani, Alessandro
  • Colosimo, Alfredo
  • Marwan, Norbert
  • Webber, Charles L.

Abstract

A statistical model describing the propensity for protein aggregation is presented. Only amino-acid hydrophobicity values and calculated net charge are used for the model. The combined effects of hydrophobic patterns as computed by the signal analysis technique, recurrence quantification, plus calculated net charge were included in a function emphasizing the effect of singular hydrophobic patches which were found to be statistically significant for predicting aggregation propensity as quantified by fluorescence studies obtained from the literature. These results suggest preliminary evidence for a mesoscopic principle for protein folding/aggregation.

Suggested Citation

  • Zbilut, Joseph P. & Mitchell, Julie C. & Giuliani, Alessandro & Colosimo, Alfredo & Marwan, Norbert & Webber, Charles L., 2004. "Singular hydrophobicity patterns and net charge: a mesoscopic principle for protein aggregation/folding," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 343(C), pages 348-358.
    • Handle: RePEc:eee:phsmap:v:343:y:2004:i:c:p:348-358
    DOI: 10.1016/j.physa.2004.05.081
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    Cited by:

    1. Facchini, Angelo & Mocenni, Chiara & Marwan, Norbert & Vicino, Antonio & Tiezzi, Enzo, 2007. "Nonlinear time series analysis of dissolved oxygen in the Orbetello Lagoon (Italy)," Ecological Modelling, Elsevier, vol. 203(3), pages 339-348.
    2. Facchini, Angelo & Rubino, Alessandro & Caldarelli, Guido & Di Liddo, Giuseppe, 2019. "Changes to Gate Closure and its impact on wholesale electricity prices: The case of the UK," Energy Policy, Elsevier, vol. 125(C), pages 110-121.

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