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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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| Главные авторы: | , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Cold Spring Harbor Laboratory Press
2004
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| Предметы: | |
| Online-ссылка: | 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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