Proteins with a high propensity to aggregate can be largely prevented from doing so with surprisingly small changes to their primary structure. By using a combination of rational design and quantitative measurements of aggregation rates, we show that adding a single charge in specific "gatekeeper" regions is sufficient to change the timescale for amyloid fibril growth from minutes to weeks, thereby dramatically reducing the efficiency of this process.
Position-dependent electrostatic protection against protein aggregation / Buell, A. K.; Tartaglia, G. G.; Birkett, N. R.; Waudby, C. A.; Vendruscolo, M.; Salvatella, X.; Welland, M. E.; Dobson, C. M.; Knowles, T. P. J.. - In: CHEMBIOCHEM. - ISSN 1439-4227. - 10:8(2009), pp. 1309-1312. [10.1002/cbic.200900144]
Position-dependent electrostatic protection against protein aggregation
Tartaglia G. G.;Vendruscolo M.;
2009
Abstract
Proteins with a high propensity to aggregate can be largely prevented from doing so with surprisingly small changes to their primary structure. By using a combination of rational design and quantitative measurements of aggregation rates, we show that adding a single charge in specific "gatekeeper" regions is sufficient to change the timescale for amyloid fibril growth from minutes to weeks, thereby dramatically reducing the efficiency of this process.| File | Dimensione | Formato | |
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