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G Ottleben

Showing results (1-10 of 4) with videos related to

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Journal of Biomolecular Structure & Dynamics|December 1, 1991
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operatorG Ottleben, L Messori, H Rüterjans, et al.
The EMBO Journal|September 1, 1994
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopyR H Fogh, G Ottleben, H Rüterjans, et al.
Proteins|March 1, 1995
A model for the LexA repressor DNA complexR M Knegtel, R H Fogh, G Ottleben, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1989
The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR studyR M Lamerichs, A Padilla, R Boelens, et al.
Pageof 1

Showing results (1-10 of 4) with videos related to

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Pageof 1
Journal of Biomolecular Structure & Dynamics|December 1, 1991
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operatorG Ottleben, L Messori, H Rüterjans, et al.
The EMBO Journal|September 1, 1994
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopyR H Fogh, G Ottleben, H Rüterjans, et al.
Proteins|March 1, 1995
A model for the LexA repressor DNA complexR M Knegtel, R H Fogh, G Ottleben, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1989
The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR studyR M Lamerichs, A Padilla, R Boelens, et al.
Pageof 1