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University of Illinois at Urbana-Champaign
The Use of High Pressure Fluorescence Spectroscopy to Investigate Subunit Interactions in Oligomeric Proteins (Neurophysin, Lac Repressor)
Abstract
dc:descriptionThe application of high hydrostatic pressures (1 atm - 3 kbar) has long been known to lead to the dissociation of oligomeric proteins due to the negative volume change accompanying this process. This technique coupled with fluorescence spectroscopy is used in this thesis in order to determine the thermodynamic constants, volume change and free energy, for dissociation equilibria of two oligomeric proteins both in absence and in presence of ligand. In this manner the effect of the ligand on the subunit interactions is determined. Two protein systems are explored using the techniques of high pressure fluorescence polarization and photon counting scanning fluorimetry.
Degree
thesis:*- 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
- 2014
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Royer, Catherine Ann
Subjects
dc:subject × 1Identifiers
dc:identifier.*- Identifier
- (UMI)AAI8600299
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/70549