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oai:www.ideals.illinois.edu:2142/84801 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gumport, Richard I. Thomas, Chad Baldo 2015-09-25T22:27:59Z 2015-09-25T22:27:59Z 10000-01-01 2003 2003 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. Made available in DSpace on 2015-09-25T22:27:59Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3101981.pdf: 6707144 bytes, checksum: 1d5fe90a89b765fc6abe72c99b05ab24 (MD5) Previous issue date: 2003 Embargo set by: Seth Robbins for item 86082 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 125 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003. http://hdl.handle.net/2142/84801 (MiAaPQ)AAI3101981 eng Chemistry, Biochemistry Structure and Biochemistry of RsrI Methyltransferase text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.