Article
A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.
FEBS letters - 18 Feb 2009
Varela Lorena, Morel Bertrand, Azuaga Ana I, Conejero-Lara Francisco
Abstract excerpt
We investigated the relationship between thermodynamic stability and amyloid aggregation propensity for a set of single mutants of the alpha-spectrin SH3 domain (Spc-SH3). Whilst mutations destabilizing the domain at position 56 did not enhance fibrillation, the N47A mutation increased the rate o...
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