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The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates

The mechanisms by which peptides and proteins form ordered aggregates are not well understood. Here we focus on the physicochemical properties of amino acids that favor ordered aggregation and suggest a parameter-free model that is able to predict the change of aggregation rates over a large set of...

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Detalhes bibliográficos
Main Authors: Tartaglia, Gian Gaetano, Cavalli, Andrea, Pellarin, Riccardo, Caflisch, Amedeo
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 2004
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2279921/
https://ncbi.nlm.nih.gov/pubmed/15169952
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.04663504
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