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The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study.
The amino-terminal DNA binding domain of LexA repressor consisting of 84 amino acid residues has been studied by two-dimensional 1H NMR. Sequence-specific 1H resonance assignments were made for the first 60 amino acid residues. The secondary structure of this part of the protein contains three alpha...
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| Autors principals: | , , , , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
1989
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC297950/ https://ncbi.nlm.nih.gov/pubmed/2780544 |
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