Investigating Ligand Induced Conformational Changes in the Estrogen Receptor

Primarily, we have investigated ER conformational structure using the reporter group method of site-directed spin labeling (SDSL), along with electron paramagnetic resonance (EPR) spectroscopy. In this work, B and C parameter calculations from EPR line-shape theory express receptor differences quantitatively as a spectrum of conformational change. Relative squared difference (RSD) analysis allows us to compare ligand receptor complexes to one another. Furthermore, a rigorous statistical analysis shows that these measurements are reproducible. Placed in context, our work helps further the development of SDSL for the examination of protein conformation, and adds significantly to the hypothesis that the ER exists in a series of dynamic conformational forms depending upon the identity of bound ligand.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Hurth, Kyle Marran

Contributors dc:contributor

• Katzenellenbogen, John A.

• Biophysics, General

Language dc:language

eng

Identifier

(MiAaPQ)AAI3202106

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84211