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. (C) 2004 Elsevier B.V. All rights reserved.
Singular hydrophobicity patterns and net charge: a mesoscopic principle for protein aggregation/folding / Joseph P., Zbilut; Julie C., Mitchell; Alessandro, Giuliani; Colosimo, Alfredo; Norbert, Marwan; Webber C., Jr. - In: PHYSICA. A. - ISSN 0378-4371. - STAMPA. - 343:1-4(2004), pp. 348-358. [10.1016/j.physa.2004.05.081]
Singular hydrophobicity patterns and net charge: a mesoscopic principle for protein aggregation/folding
COLOSIMO, Alfredo;
2004
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. (C) 2004 Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
