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Dissociation of intermolecular disulfide bonds in P22 tailspike protein intermediates in the presence of SDS
Each chain of the native trimeric P22 tailspike protein has eight cysteines that are reduced and buried in its hydrophobic core. However, disulfide bonds have been observed in the folding pathway and they are believed to play a critical role in the registration of the three chains. Interestingly, in...
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| Main Authors: | , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
2006
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| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2040104/ https://ncbi.nlm.nih.gov/pubmed/16751612 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.062197206 |
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