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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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| Udgivet i: | PLoS One |
|---|---|
| Main Authors: | , , , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Public Library of Science
2014
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4260792/ https://ncbi.nlm.nih.gov/pubmed/25490095 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0113224 |
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