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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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| Hoofdauteurs: | , , , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Cold Spring Harbor Laboratory Press
2004
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| Onderwerpen: | |
| Online toegang: | 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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