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https://hdl.handle.net/2142/84900
Description
Title
Stability and Dynamics of Apocytochrome B(562)
Author(s)
Fuentes, Ernesto Jorge
Issue Date
1999
Doctoral Committee Chair(s)
Wand, A. Joshua
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
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.
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