Protein Aggregation/Folding: The Role of Deterministic Singularities of Sequence Hydrophobicity as Determined by Nonlinear Signal Analysis of Acylphosphatase and Aβ(1-40)

38Citations
Citations of this article
42Readers
Mendeley users who have this article in their library.

Abstract

The problem of protein folding vs. aggregation was investigated in acylphosphatase and the amyloid protein Aβ(1-40) by means of nonlinear signal analysis of their chain hydrophobicity. Numerical descriptors of recurrence patterns provided the basis for statistical evaluation of folding/aggregation distinctive features. Static and dynamic approaches were used to elucidate conditions coincident with folding vs. aggregation using comparisons with known protein secondary structure classifications, site-directed mutagenesis studies of acylphosphatase, and molecular dynamics simulations of amyloid protein, Aβ(1-40). The results suggest that a feature derived from principal component space characterized by the smoothness of singular, deterministic hydrophobicity patches plays a significant role in the conditions governing protein aggregation.

Cite

CITATION STYLE

APA

Zbilut, J. P., Colosimo, A., Conti, F., Colafranceschi, M., Manetti, C., Valerio, M. C., … Giuliani, A. (2003). Protein Aggregation/Folding: The Role of Deterministic Singularities of Sequence Hydrophobicity as Determined by Nonlinear Signal Analysis of Acylphosphatase and Aβ(1-40). Biophysical Journal, 85(6), 3544–3557. https://doi.org/10.1016/S0006-3495(03)74774-2

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free