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Wand, A. Joshua Fuentes, Ernesto Jorge 2015-09-25T22:28:24Z 2015-09-25T22:28:24Z 10000-01-01 1999 1999 The dependence of the global unfolding free energy upon denaturant concentration indicates the applicability of a binding model and explains the observed difference between global unfolding free energies obtained by the linear extrapolation method and those obtained by calorimetry and hydrogen exchange. The dependence of the global unfolding free energy upon pressure is first order and associated with a negative volume change of -105 mL mol-1. The two additional regions of cooperative structure also displayed negative volume changes associated with their unfolding, albeit smaller in magnitude. Surprisingly, one of the subglobal unfolding units shows a significant positive volume change at low pressures (<200 bar) suggesting the presence of a highly mispacked open state at ambient pressure. These observations place a significant restraint upon the type of folding pathway that is operative for this protein and suggest that that the N- and C-terminal helices fold and unfold independently of the core of the molecule. Made available in DSpace on 2015-09-25T22:28:24Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9921688.pdf: 4011407 bytes, checksum: f78bf5e2d5ae14f5f950d786781bb776 (MD5) Previous issue date: 1999 Embargo set by: Seth Robbins for item 86181 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 146 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999. http://hdl.handle.net/2142/84900 (MiAaPQ)AAI9921688 eng Biology, Molecular Stability and Dynamics of Apocytochrome B(562) text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.