{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84801"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84801","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Structure and Biochemistry of RsrI Methyltransferase","abstract":"Comparison of the dimer interface of M.RsrI with the recent M.MboII structure and sequence alignments allowed identification of a conserved dimerization motif. I disrupted the dimerization of M.RsrI by adding N-acetyl-phenylalanine as a competitive inhibitor and by mutation of a serine located in the dimer interface to an aspartate. Both methods resulted in inhibition of the enzyme activity, suggesting dimerization is important for enzyme activity.","abstract_html":"Comparison of the dimer interface of M.RsrI with the recent M.MboII structure and sequence alignments allowed identification of a conserved dimerization motif. I disrupted the dimerization of M.RsrI by adding N-acetyl-phenylalanine as a competitive inhibitor and by mutation of a serine located in the dimer interface to an aspartate. 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I disrupted the dimerization of M.RsrI by adding N-acetyl-phenylalanine as a competitive inhibitor and by mutation of a serine located in the dimer interface to an aspartate. Both methods resulted in inhibition of the enzyme activity, suggesting dimerization is important for enzyme activity.","Made available in DSpace on 2015-09-25T22:27:59Z (GMT). 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I disrupted the dimerization of M.RsrI by adding N-acetyl-phenylalanine as a competitive inhibitor and by mutation of a serine located in the dimer interface to an aspartate. Both methods resulted in inhibition of the enzyme activity, suggesting dimerization is important for enzyme activity.","Made available in DSpace on 2015-09-25T22:27:59Z (GMT). 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