A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state

FEBS Letters

Volumn 583, Issue 4, 2009, Pages 801-806

  Varela, Lorena ^a   Morel, Bertrand ^a   Azuaga, Ana I ^a   Conejero Lara, Francisco ^a  

^a UNIVERSITY OF GRANADA   (Spain)

Author keywords

Amyloid; Differential scanning calorimetry; Dynamic light scattering; Protein stability; Thermodynamics

Indexed keywords

AMYLOID; FODRIN; MUTANT PROTEIN; PROTEIN SH3;

ARTICLE; GENE MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; THERMODYNAMICS;

AMYLOID; MUTATION; PROTEIN CONFORMATION; SRC HOMOLOGY DOMAINS; TEMPERATURE; THERMODYNAMICS; TIME FACTORS;

EID: 59849130063     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.01.033     Document Type: Article

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