TY  - JOUR
A1  - Zbilut, J. P.
A1  - Giuliani, A.
A1  - Colosimo, A.
A1  - Mitchell, J. C.
A1  - Colafranceschi, M.
A1  - Marwan, Norbert
A1  - Webber, C. L.
A1  - Uversky, V. N.
T1  - Charge and hydrophobicity patterning along the sequence predicts the folding mechanism and aggregation of proteins : a computational approach
N2  - The presence of partially folded intermediates along the folding funnel of proteins has been suggested to be a signature of potentially aggregating systems. Many studies have concluded that metastable, highly flexible intermediates are the basic elements of the aggregation process. In a previous paper, we demonstrated how the choice between aggregation and folding behavior was influenced by hydrophobicity distribution patterning along the sequence, as quantified by recurrence quantification analysis (RQA) of the Myiazawa-Jernigan coded primary structures. In the present paper, we tried to unify the "partially folded intermediate" and "hydrophobicity/charge" models of protein aggregation verifying the ability of an empirical relation, developed for rationalizing the effect of different mutations on aggregation propensity of acyl-phosphatase and based on the combination of hydrophobicity RQA and charge descriptors, to discriminate in a statistically significant way two different protein populations: (a) proteins that fold by a process passing by partially folded intermediates and (b) proteins that do not present partially folded intermediates
Y1  - 2004
SN  - 1535-3893
ER  - 
TY  - JOUR
A1  - Zbilut, J. P.
A1  - Mitchell, J. C.
A1  - Giuliani, A.
A1  - Colosimo, A.
A1  - Marwan, Norbert
A1  - Webber, C. L.
T1  - Singular hydrophobicity patterns and net charge : a mesoscopic principle for protein aggregation/folding
N2  - 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
Y1  - 2004
SN  - 0378-4371
ER  -