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

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

Physica A: Statistical Mechanics and its Applications, 2004, vol. 343, issue C, 348-358

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.

Keywords: Singularities; Protein; Aggregation; Folding; Recurrence analysis; Mesoscopic (search for similar items in EconPapers)
Date: 2004
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Citations: View citations in EconPapers (2)

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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:343:y:2004:i:c:p:348-358

DOI: 10.1016/j.physa.2004.05.081

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