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Kelleher, Neil L. Mazur, Matthew Thomas 2015-09-25T22:13:14Z 2015-09-25T22:13:14Z 10000-01-01 2004 2004 This is the first in-depth application of FTMS to the study of NRP/PKS enzymes for the elucidation of natural product biosynthesis. The reliance of FTMS will continue to improve and should prove itself worthy of the best analytical assay tool for uncovering the intricate mechanisms of thiotemplate enzymes. Made available in DSpace on 2015-09-25T22:13:14Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3153377.pdf: 8182615 bytes, checksum: 7dd9cc66e2559e6c0e1ab8f56d30aa72 (MD5) Previous issue date: 2004 Embargo set by: Seth Robbins for item 85439 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 111 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2004. http://hdl.handle.net/2142/84158 (MiAaPQ)AAI3153377 eng Chemistry, Biochemistry Mass Spectrometric Studies of Nonribosomal, Enzymatic Assembly of Natural Products Through Thiotemplate Biosynthesis text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.