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• W1972634576 endingPage "816" @default.
• W1972634576 startingPage "811" @default.
• W1972634576 abstract "The MetJ repressor is the archetypal example of the beta-ribbon-helix-helix DNA binding motif. A model of the MetJ beta-ribbon (residues 22-28) was prepared by forming a dityrosine crosslinked dimer from the heptapeptide KKYTVSI. Using SPR, the peptide dimer 2 was shown to bind to dsDNA under physiologically relevant conditions, whereas the monomeric peptide did not. The peptide dimer appeared to inhibit binding of the MetJ repressor to natural met operators. Based on the stoichiometry of binding, the binding of peptide dimer 2 seems both highly co-operative and to lack sequence specificity. Peptide binding also appears to prevent transcription in vitro." @default.
• W1972634576 created "2016-06-24" @default.
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• W1972634576 date "2003-03-01" @default.
• W1972634576 modified "2023-09-26" @default.
• W1972634576 title "A biaryl peptide crosslink in a MetJ peptide model confers cooperative, nonspecific binding to DNA that ablates both repressor binding and In vitro transcription" @default.
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• W1972634576 doi "https://doi.org/10.1016/s0968-0896(02)00583-7" @default.
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