Matthew Skeels

Associate Professor Chemistry Department
Matthew Skeels

Teaching Interests

general chemistry, quantitative analysis, bio-analytical chemistry, instrumental analysis, environmental chemistry, and biochemistry.

Research Interests

  • Protein folding. Understanding the mechanism by which proteins acquire their precisely folded three-dimensional structures remains one of the most important challenges of structural biology. To solve this complex problem, a variety of experimental techniques as well as computational methods of analysis are used to probe the role of different interactions in protein folding and protein interactions with ligands. Answers to the protein-folding problem play a key role in designing proteins with new functional properties and improved methods for protein structure prediction. Moreover, a thorough understanding of the principles that govern folding of proteins in vitro is a prerequisite for elucidating protein folding in the cell, which has far-reaching biological and medical implications.
  • Medicinally relevant alkaloids. Current research is focused on the development, validation, and application of HPLC methods to test for medicinally relevant pharmaceutical products in ethnopharmaceuticals. Current research collaboration with Dr. Aswini Pai in biology include assessing the concentration of isoquinoline alkaloids in Hydrastis canadensis.
  • Androgen Receptor. In mammals, natural testosterones play a critical role in the normal development and function of the sex organs in males and the maintenance of spermatogenesis. The actions of androgens are mediated by the androgen receptor (AR). These receptors have distinct domains for DNA binding, ligand binding, and transcriptional activation. When androgens bind to the androgen receptor, a change takes place causing dissociation of the androgen receptor/DNA complex and results in transcriptional activation. Androgen activation is strongly linked to prostate cancer. The unique requirement of androgens to maintain the growth of the tumor and evade apoptosis is the basis for androgen blocking therapies. Because androgen bound to the androgen receptor is completely enveloped by protein, it is thought that the process of ligand binding or unbinding must involve a significant conformational change. Probing the mechanism of ligand binding and release can have far reaching consequences toward drug design that targets certain types of prostate cancer.

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