Stability and Dynamics of Apocytochrome B(562)

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Fuentes, Ernesto Jorge

Contributors dc:contributor

• Wand, A. Joshua

• Biology, Molecular

Language dc:language

eng

Identifier

(MiAaPQ)AAI9921688

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84900