Journal
PHYSICAL REVIEW LETTERS
Volume 104, Issue 22, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.104.228101
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Funding
- U.K. EPSRC
- IRC in Nanotechnology
- Nokia Research
- St. John's College and Magdalene College, Cambridge
- Engineering and Physical Sciences Research Council [GR/R45680/01, EP/F032773/1] Funding Source: researchfish
- Medical Research Council [qA137861b] Funding Source: researchfish
- EPSRC [EP/F032773/1] Funding Source: UKRI
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Using quantitative measurements of protein aggregation rates, we develop a kinetic picture of protein conversion from a soluble to a fibrillar state which shows that a single free energy barrier to aggregation controls the addition of protein molecules into amyloid fibrils, while the characteristic sublinear concentration dependence emerges as a natural consequence of finite diffusion times. These findings suggest that this reaction does not follow a simple chemical mechanism, but rather operates in a way analogous to the landscape models of protein folding defined by stochastic dynamics on a characteristic energy surface.
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