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Annual Review of Physical Chemistry

Volume 66, 2015

Computational Studies of Protein Aggregation: Methods and Applications

Abstract

Protein aggregation involves the self-assembly of normally soluble proteins into large supramolecular assemblies. The typical end product of aggregation is the amyloid fibril, an extended structure enriched in β-sheet content. The aggregation process has been linked to a number of diseases, most notably Alzheimer's disease, but fibril formation can also play a functional role in certain organisms. This review focuses on theoretical studies of the process of fibril formation, with an emphasis on the computational models and methods commonly used to tackle this problem.

Keyword(s): amyloid fibrils, coarse-grained models, enhanced sampling methods, molecular dynamics simulations, replica exchange molecular dynamics, systematic coarse graining
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2015-04-01
2024-06-07
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Computational Studies of Protein Aggregation: Methods and Applications
Annual Review of Physical Chemistry 66, 643 (2015); https://doi.org/10.1146/annurev-physchem-040513-103738
/content/journals/10.1146/annurev-physchem-040513-103738
/content/journals/10.1146/annurev-physchem-040513-103738
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