期刊
FEBS LETTERS
卷 583, 期 4, 页码 801-806出版社
WILEY
DOI: 10.1016/j.febslet.2009.01.033
关键词
Amyloid; Thermodynamics; Protein stability; Differential scanning calorimetry; Dynamic light scattering
资金
- Andalucia Regional Governmen [FQM-00123, FQM-02838]
- Spanish Ministry of Education and Science [BIO2006-15517.C02.01]
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 of amyloid. fibril formation by 10-fold. Even under conditions of identical thermodynamic stability, the aggregation rate was much higher for the N47A mutant than for the WT domain. We conclude that the N47A mutation does not change the apparent mechanism of. fibrillation or the morphology of the amyloid. fibrils, and that its amyloidogenic property is due to its effect upon the rate of the conformational events leading to nucleation and not to its overall destabilizing effect. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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