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Rationally designed helix-turn-helix proteins and their conformational changes upon DNA binding.
Circular dichroism and electrophoretic mobility shift studies were performed to confirm that dimerized N-terminal domains of bacterial repressors containing helix-turn-helix motifs are capable of high-affinity and specific DNA recognition as opposed to the monomeric N-terminal domains. Specific, hig...
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| Hoofdauteurs: | , , , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1995
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC394381/ https://ncbi.nlm.nih.gov/pubmed/7621832 |
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