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Sligar, Stephen G. Jonas, Jiri Bondos, Sarah Elizabeth 2015-09-25T22:28:23Z 2015-09-25T22:28:23Z 10000-01-01 1998 1998 Four mutations were also examined to determine how specific packing defects affect high pressure denaturation. Mutations were made in three positions in the core to determine how the position contributes to changes in stability. Also, charged and oversized residues were introduced into the core to determine how particular types of defects affect the pressure stability of the native and high pressure intermediate states. The effects of mutation are shown to be more dependent on the nature of the mutation, with charge burial mutations being the most deleterious given that all positions are buried in the AGH core. Made available in DSpace on 2015-09-25T22:28:23Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9912197.pdf: 5366519 bytes, checksum: 21c8fe61782650d15c0cea3b72588a6c (MD5) Previous issue date: 1998 Embargo set by: Seth Robbins for item 86176 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 116 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998. http://hdl.handle.net/2142/84895 (MiAaPQ)AAI9912197 eng Chemistry, Biochemistry High Pressure Protein Denaturation: Description of a High Pressure Intermediate and Effects of Mutations on Pressure Stability text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.