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Hexa-histidin tag position influences disulfide structure but not binding behavior of in vitro folded N-terminal domain of rat corticotropin-releasing factor receptor type 2a

The oxidative folding, particularly the arrangement of disulfide bonds of recombinant extracellular N-terminal domains of the corticotropin-releasing factor receptor type 2a bearing five cysteines (C2 to C6), was investigated. Depending on the position of a His-tag, two types of disulfide patterns w...

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Detalhes bibliográficos
Main Authors: Klose, Jana, Wendt, Norbert, Kubald, Sybille, Krause, Eberhard, Fechner, Klaus, Beyermann, Michael, Bienert, Michael, Rudolph, Rainer, Rothemund, Sven
Formato: Artigo
Idioma:English
Publicado em: Cold Spring Harbor Laboratory Press 2004
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2280012/
https://ncbi.nlm.nih.gov/pubmed/15295109
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.04835904
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