The extreme hyper-reactivity of Cys94 in lysozyme avoids its amorphous aggregation

Many proteins provided with disulfide bridges in the native state undergo amorphous irreversible aggregation when these bonds are not formed. Here we show that egg lysozyme displays a clever strategy to prevent this deleterious aggregation during the nascent phase when disulfides are still absent. I...

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Detalles Bibliográficos
Autores principales: Bocedi, Alessio, Cattani, Giada, Martelli, Claudia, Cozzolino, Flora, Castagnola, Massimo, Pucci, Pietro, Ricci, Giorgio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6207692/
https://www.ncbi.nlm.nih.gov/pubmed/30375487
http://dx.doi.org/10.1038/s41598-018-34439-y

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6207692/
https://www.ncbi.nlm.nih.gov/pubmed/30375487
http://dx.doi.org/10.1038/s41598-018-34439-y

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