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pubmed-article:12405833pubmed:abstractTextTypical eukaryotic transcriptional activators are composed of distinct functional domains, including a DNA binding domain and an activating domain. Artificial transcription factors have been designed wherein the DNA binding domain is a minor groove DNA binding hairpin polyamide linked by a flexible tether to short activating peptides, typically 16-20 residues in size. In this study, the linker between the polyamide and the peptide was altered in an incremental fashion using rigid oligoproline "molecular rulers" in the 18-45 A length range. We find that there is an optimal linker length which separates the DNA and the activation region for transcription activation.lld:pubmed
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pubmed-article:12405833pubmed:articleTitleDesign of artificial transcriptional activators with rigid poly-L-proline linkers.lld:pubmed
pubmed-article:12405833pubmed:affiliationDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.lld:pubmed
pubmed-article:12405833pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12405833pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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