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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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| Publicado no: | Proc Natl Acad Sci U S A |
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| Main Authors: | , , , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1989
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC297950/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2780544/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.18.6863 |
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