Publication: Crowding effects on amyloid aggregation kinetics
Crowding effects on amyloid aggregation kinetics
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Magno, A., Caflisch, A., & Pellarin, R. (2010). Crowding effects on amyloid aggregation kinetics. Journal of Physical Chemistry Letters, 1, 3027–3032. https://doi.org/10.1021/jz100967z
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Biological protein self-assembly occurs in the cellular milieu, densely occupied by other macromolecules which do not participate directly in the aggregation process. Excluded volume effects arising in such a crowded environment deeply affect the thermodynamics and kinetics of biological processes, like protein folding, ligand binding, and protein aggregation. Here, Langevin dynamics simulations of a simplified model of an amphipathic polypeptide are used to investigate how macromolecular crowding influences the amyloid aggregation ki
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- Magno, A
- Caflisch, A
- Pellarin, R
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Citations
Magno, A., Caflisch, A., & Pellarin, R. (2010). Crowding effects on amyloid aggregation kinetics. Journal of Physical Chemistry Letters, 1, 3027–3032. https://doi.org/10.1021/jz100967z
