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“Reduction of the C191-C220 disulfide of α-chymotrypsinogen A reduces nucleation barriers for aggregation”
Proper disulfide formation can be essential for the conformational stability of natively folded proteins. For proteins that must unfold in order to aggregate, disruption of native disulfides may therefore promote aggregation. This study characterizes differences in the aggregation process for wild-t...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2013
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4108794/ https://ncbi.nlm.nih.gov/pubmed/24374388 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpc.2013.11.005 |
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