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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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Bibliografiske detaljer
Main Authors: Kim, Junghwa, Robinson, Anne Skaja
Format: Artigo
Sprog:Inglês
Udgivet: Cold Spring Harbor Laboratory Press 2006
Fag:
Online adgang: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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