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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Hlavní autoři: Lamerichs, R M, Padilla, A, Boelens, R, Kaptein, R, Ottleben, G, Rüterjans, H, Granger-Schnarr, M, Oertel, P, Schnarr, M
Médium: Artigo
Jazyk:Inglês
Vydáno: 1989
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Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC297950/
https://ncbi.nlm.nih.gov/pubmed/2780544
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