Theses and Dissertations

Date of Award


Document Type


Degree Name

Master of Science (MS)



First Advisor

Dr. Evangelia Kotsikorou

Second Advisor

Dr. Frank Dean

Third Advisor

Dr. Jason Parsons


The androgen receptor (AR) can be activated by molecules binding in the steroid binding pocket. It can also be regulated allosterically by cofactors binding to the AF-2 surface site as well as by exogenous small molecules binding to the BF-3 surface site. Recent data indicated that mutations in the BF-3 site changed the amount of the endogenous steroid needed to activate the receptor, indicating that mutations of BF-3 can cause an allosteric effect. Molecular dynamics and steered molecular dynamics simulations were used to study the allosteric effect of the mutations on AR structure and the unbinding pathways of testosterone (TES) from AR. It was found that the BF-3 mutations did not have the destabilizing effect expected. However, the mutations resulted in changes of the hydrogen bonding patterns for TES bound in the steroid binding pocket as well as differences in the unbinding pathways for TES.


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