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FEBS Letters|June 11, 1984
Cooperative and salt-resistant binding of lexA protein to non-operator DNAM Schnarr, M DauneEuropean Journal of Biochemistry|August 15, 1989
Investigation of RecA--polynucleotide interactions from the measurement of LexA repressor cleavage kinetics. Presence of different types of complexM Takahashi, M SchnarrBiochimica Et Biophysica Acta|April 3, 1982
Stability of the lac repressor headpiece against thermal denaturation and tryptic hydrolysisM Schnarr, J C MaurizotEuropean Journal of Biochemistry|November 15, 1982
Secondary structure of the lac repressor headpiece. Possibilities and limitations of a joint infrared and circular dichroism studyM Schnarr, J C MaurizotBiochemistry|October 13, 1981
Unfolding of lac repressor and its proteolytic fragment by urea: headpieces stabilize the core within lac repressorM Schnarr, J C MaurizotFEBS Letters|February 17, 1986
Fluorescence study of the RecA-dependent proteolysis of LexA, the repressor of the SOS system in Escherichia coliM Takahashi, M Daune, M SchnarrBiochemistry|February 20, 1990
The LexA repressor and its isolated amino-terminal domain interact cooperatively with poly[d(A-T)], a contiguous pseudo-operator, but not with random DNA: a circular dichroism studyS Hurstel, M Granger-Schnarr, M SchnarrFEBS Letters|April 25, 1988
A mutant LexA repressor harboring a cleavage motif cysteine-glycine remains inducibleM Granger-Schnarr, P Oertel, M SchnarrBiochemistry|July 19, 1983
Nonspecific interaction of the lac repressor headpiece with deoxyribonucleic acid: fluorescence and circular dichroism studiesM Schnarr, M Durand, J C MaurizotThe EMBO Journal|January 1, 1982
Interaction between the lac operator and the lac repressor headpiece: fluorescence and circular dichroism studiesF Culard, M Schnarr, J C MaurizotPageof 6