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Computational Modeling of Biological Systems pp 215–227Cite as

The Structure of Intrinsically Disordered Peptides Implicated in Amyloid Diseases: Insights from Fully Atomistic Simulations

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Part of the book series: Biological and Medical Physics, Biomedical Engineering ((BIOMEDICAL))

Abstract

Protein aggregation involves the self-assembly of proteins into large β-sheet-rich complexes. This process can be the result of aberrant protein folding and lead to “amyloidosis,” a condition characterized by deposits of protein aggregates known as amyloids on various organs of the body [1]. Amyloid-related diseases include, among others, Alzheimer’s disease, Parkinson’s disease, Creutzfeldt–Jakob disease, and type II diabetes [2, 3, 4]. In other instances, however, protein aggregation is not a pathological process, but rather a functional one, with aggregates serving as structural scaffolds in a number of organisms [5].

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Acknowledgments

This work was funded by the David and Lucile Packard Foundation, the NSF (MCB 0642086), and the NIH (AG027818). The computing time was provided by the Lonestar and Ranger clusters in the Texas Advanced Computing Center (LRAC MCA 05S027).

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  1. Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, 93106, USA

    Chun Wu

  2. Department of Physics, University of California, Santa Barbara, CA, 93106, USA

    Joan-Emma Shea

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Wu, C., Shea, JE. (2012). The Structure of Intrinsically Disordered Peptides Implicated in Amyloid Diseases: Insights from Fully Atomistic Simulations. In: Dokholyan, N. (eds) Computational Modeling of Biological Systems. Biological and Medical Physics, Biomedical Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-2146-7_9

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