Electrostatic Effects in the Folding of the SH3 Domain of the c-Src Tyrosine Kinase: pH-Dependence in 3D-Domain Swapping and Amyloid Formation

The SH3 domain of the c-Src tyrosine kinase (c-Src-SH3) aggregates to form intertwined dimers and amyloid fibrils at mild acid pHs. In this work, we show that a single mutation of residue Gln128 of this SH3 domain has a significant effect on: (i) its thermal stability; and (ii) its propensity to for...

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Detalles Bibliográficos
Autores principales: Bacarizo, Julio, Martinez-Rodriguez, Sergio, Martin-Garcia, Jose Manuel, Andujar-Sanchez, Montserrat, Ortiz-Salmeron, Emilia, Neira, Jose Luis, Camara-Artigas, Ana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4260792/
https://www.ncbi.nlm.nih.gov/pubmed/25490095
http://dx.doi.org/10.1371/journal.pone.0113224

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4260792/
https://www.ncbi.nlm.nih.gov/pubmed/25490095
http://dx.doi.org/10.1371/journal.pone.0113224

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