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Geil, Phillip H. Wang, Jinfeng 2015-09-25T20:52:54Z 2015-09-25T20:52:54Z 10000-01-01 2004 2004 In the second part, the molecular composition, size and conformation of zein, corn prolamines, was examined with MALDI-MS, TEM, SEC3, SAXS and viscometry. MALDI-MS is demonstrated to be a superior technique to study the molecular weight and composition of zein proteins than conventional SDS-PAGE. The observed large particle size from TEM and SEC3 compared to the predicted value from the molecular weight suggested that zein tends to form oligomeric structures. The denaturation behavior of zero was also studied using various denaturants. The results showed most denaturation agents, such as pH, guanidine hydrochloride and DTT, didn't denature zein. Temperature and SDS may cause some denaturation as suggested from the increase of the intrinsic viscosity; the change of intrinsic viscosity was not sufficient to indicate coil-like conformation. Made available in DSpace on 2015-09-25T20:52:54Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3160966.pdf: 13569294 bytes, checksum: 375db0d69002c86841d9abb883ace5a3 (MD5) Previous issue date: 2004 Embargo set by: Seth Robbins for item 84040 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 147 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2004. http://hdl.handle.net/2142/82759 (MiAaPQ)AAI3160966 eng Chemistry, Polymer Structural Study of Natural and Synthetic Polymers text Materials Science and Engineering Materials Science and Engineering University of Illinois at Urbana-Champaign Dissertation Ph.D.