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...

Полное описание

Библиографические подробности

Опубликовано в::	Proc Natl Acad Sci U S A
Главные авторы:	Lamerichs, R M, Padilla, A, Boelens, R, Kaptein, R, Ottleben, G, Rüterjans, H, Granger-Schnarr, M, Oertel, P, Schnarr, M
Формат:	Artigo
Язык:	Inglês
Опубликовано:	National Academy of Sciences 1989
Предметы:	Research Article
Online-ссылка:	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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