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; Charles L. Webber

doi:10.1016/j.physa.2004.05.081

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, Charles L. Webber

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

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.

Original language	English
Pages (from-to)	348-358
Number of pages	11
Journal	Physica A: Statistical Mechanics and its Applications
Volume	343
Issue number	1-4
DOIs	https://doi.org/10.1016/j.physa.2004.05.081
State	Published - Nov 15 2004
Externally published	Yes

Funding

This work was supported by a joint DMS/NIGMS initiative to support mathematical biology, from the National Science Foundation and National Institutes of Health, (NSF DMS 0240230); J.P. Zbilut, Principal Investigator.

Funders	Funder number
NSF DMS	0240230
National Science Foundation
National Institutes of Health
National Institute of General Medical Sciences
Division of Mathematical Sciences

Keywords

Aggregation
Folding
Mesoscopic
Protein
Recurrence analysis
Singularities

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10.1016/j.physa.2004.05.081

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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.",

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T2 - A mesoscopic principle for protein aggregation/folding

AU - Zbilut, Joseph P.

AU - Mitchell, Julie C.

AU - Giuliani, Alessandro

AU - Colosimo, Alfredo

AU - Marwan, Norbert

AU - Webber, Charles L.

PY - 2004/11/15

Y1 - 2004/11/15

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AB - 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.

KW - Aggregation

KW - Folding

KW - Mesoscopic

KW - Protein

KW - Recurrence analysis

KW - Singularities

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JO - Physica A: Statistical Mechanics and its Applications

JF - Physica A: Statistical Mechanics and its Applications

IS - 1-4

ER -

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

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Keywords

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