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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