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Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity
Although high affinity binding between streptavidin and biotin is widely exploited, the accompanying low rate of dissociation prevents its use in many applications where rapid ligand release is also required. To combine extremely tight and reversible binding, we have introduced disulfide bonds into...
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| Vydáno v: | Sci Rep |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Publishing Group UK
2020
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7385176/ https://ncbi.nlm.nih.gov/pubmed/32719366 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-020-69357-5 |
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